POLG_LMV0
ID POLG_LMV0 Reviewed; 3255 AA.
AC P31999; P90263;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
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 Lettuce mosaic virus (strain 0 / isolate French) (LMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117132;
OH NCBI_TaxID=4222; Carthamus tinctorius (Safflower).
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH NCBI_TaxID=114280; Cichorium endivia (Endive).
OH NCBI_TaxID=13427; Cichorium intybus (Chicory).
OH NCBI_TaxID=52518; Eustoma exaltatum subsp. russellianum (Bluebells) (Eustoma grandiflorum).
OH NCBI_TaxID=4235; Lactuca.
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9085548; DOI=10.1016/s0168-1702(96)01411-6;
RA Revers F., Yang S.J., Walter J., Souche S., Lot H., Le Gall O.,
RA Candresse T., Dunez J.;
RT "Comparison of the complete nucleotide sequences of two isolates of lettuce
RT mosaic virus differing in their biological properties.";
RL Virus Res. 47:167-177(1997).
RN [2]
RP SEQUENCE REVISION TO 1750 AND 1771.
RA Le Gall O.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2776-3255.
RX PubMed=2001176; DOI=10.1007/bf01319245;
RA Dinant S., Lot H., Albouy J., Kuziak C., Meyer M., Astier-Manifacier S.;
RT "Nucleotide sequence of the 3' terminal region of lettuce mosaic potyvirus
RT RNA shows a Gln/Val dipeptide at the cleavage site between the polymerase
RT and the Capsid protein.";
RL Arch. Virol. 116:235-252(1991).
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=P31999-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CJ97-1; 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; X97704; CAA66280.2; -; mRNA.
DR EMBL; X65652; CAA46602.1; -; Genomic_RNA.
DR PIR; S70859; S70859.
DR Proteomes; UP000008377; 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 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..3255
FT /note="Genome polyprotein"
FT /id="PRO_0000419999"
FT CHAIN 1..437
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040269"
FT CHAIN 438..895
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040270"
FT CHAIN 896..1273
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040271"
FT CHAIN 1274..1325
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040272"
FT CHAIN 1326..1968
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040273"
FT CHAIN 1969..2021
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040274"
FT CHAIN 2022..2214
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040275"
FT CHAIN 2215..2457
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040276"
FT CHAIN 2458..2977
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040277"
FT CHAIN 2978..3255
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040278"
FT DOMAIN 292..437
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 773..895
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1397..1549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1568..1727
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2215..2433
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2699..2823
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2980..3028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 489..492
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 747..749
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1499..1502
FT /note="DECH box"
FT MOTIF 2062..2069
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2980..3002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3012..3026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 354
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 388
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 781
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 854
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2260
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2295
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2365
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1410..1417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 437..438
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 895..896
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1273..1274
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1325..1326
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1968..1969
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 2214..2215
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2457..2458
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2977..2978
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 2084
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3255 AA; 367571 MW; 763F676F95876A12 CRC64;
MATLDNCTQV HHMFAYNREH GTNYTRNHFR RYLAAQRIGF YYDWDDDVYE CPTCEAIYHS
LDDIKNWHEC DPPAFDLNDF ITDARLKSAP VPDLGPVIIE IPKAEEKQEL NFFAATPAPE
VSQWKCRGLQ FGSFTELETS EPVASAPEPK CEEPARTIAK PEESVEQETR GDGKRLLQAQ
MEVDKAEQDL AFACLNASLK PRLEGRTTAT IARRRDGCLV YKTKPSWSQR RRAKKTLKVD
TLACENPYIP AIVDKISIAG GSSASVMHEQ QKPKTLHTTP SRKVATHYKR TVMNQQTLMA
FINQVGTILL NAEKEFEVVG CRKQKVTGKG TRHNGVRLVK LKTAHEEGHR RRVDIRIPNG
LRPIVMRISA RGGWHRTWTD SELSPGSSGY VLNSSKIIGK FGLRRHSIFV VRGRVDGEVI
DSQSKVTHSI THRMVQYSDV ARNFWNGYST CFMHNTPKDI LHTCTSDFDV KECGTVAALL
TQTLFQFGKI TCEKCAIEYK NLTRDELATR VNKEIDGTII SIQTQHPRFV HVLNFLRLIK
QVLNAKNGNF GAFQETERII GDRMDAPFSH VNKLNAIVIK GNQATSDEMA QASNHVLEIA
RYLKNRTENI QKGSLKSFRN KISGKAHLNP SLMCDNQLDK NGGFEWGQRS YHAKRFFDGY
FETIDPSDGY SKYTIRRNPN GHRKLAIGNL IVSTNFESHR RSMIGESIED PGLTNQCVSK
EGDTFIYPCC CVTDEYGKPT LSEIKMPTKH HLVLGNAGDP KYVDLPKEAE GKMFVTKDGY
CYINIFLAML VDVPEDQAKD FTKMAREIAV KQLGEWPSMM DVATACNILA TFHPDTRRSE
LPRILVDHAT KTFHVIDSYG SITTGFHILK ANTVTQLVKF AHESLESEMQ HYRVGGEPDK
APRKPAGSVP TLGISDLRDL GVELENEEHS IRPNLQRLIK AIYRPRMMRS LLTEEPYLLI
LSIVSPGVLM ALYNSGSLER TMHEFLQTDQ RLSATAQILK HLAKKVSLAK TLTIQNAILE
GGAGSLNEIL DAPAGRSLSY RLAKQTVEVM MARSDMDKEL VDVGFSVLRD QKNELIEKSY
LMDLEDSWHA LPLCGKLSAM RASRRWRDTS TPEVIPTGAA DLKGRYSISV GSVSKSAILH
LKGICSGAVK RVRDKWVGVQ VQGVKWLAKS VHYMIPELTN ILNVGTLLLT LISLGVAFRN
LTGQFKEMKH KETLAKEEEL RKRIRTYNST YYEIHGKHAD AKQITKFITH HDPKLLEVVE
FYEGPEEEEV EHQAKREDQA NLERIIAFTA LVMMMFDSER SDCVYRSLSK LKSLVSTCED
DVRHQSVDEI IDLFDEKKET IDFEIEGKEL YSSRVVDSTF SKWWDNQLVR GNTMAHYRTE
GHFMTFTRET AASVAAEIAH NEYRDILLQG GVGSGKSTGL PFHLHRKGGV LLIEPTRPLA
QNVYKQLGSS PFHLSPNLRM RGSCKFGSSQ VTVATSGYAL HFIANNAQSL KAYDFIIFDE
CHVLDASAMA FRCLLQEFEY QGKIIKVSAT PPGRKLDFKP MHMVDIATEN ELSIQQFVQG
QGTGVNCDAT KKGDNILVYV SSYNEVDMLS KMLNDKGYKV TKVDGRTMKL GSVEVETVGT
PQRKHFVVAT NIIENGVTLD VDVVVDFGQK VVPILDSEHR MIRYTKKSIT YGERIQRVGR
VGRNKAGSAI RIGSTEMGTE EIPASIATEA AFLCFTYGLP VMTSNVSTSV LGNCTVRQAR
TMQKFELSPF FMVDLVHHDG TIHPAINSLL KQFKLKESDI KLSTLAIPNA VTTFWKSARE
YNSLGARTTI DDAAKIPFMI KDVPEHLQEK LWETIQQYKG DAGFGRCTSA NACKIAYTLS
VSPFMIPATI NKIDALMAEE RQKMEYFQTV TANTCTISNF SISSIGDMIR SRYSTNHSRE
NLQKLQAVRD TIINFECQAG TGDGGSFDME TAQKLAEEYG CIDVIYHQSK EALSKRLGLK
GRWNQSLICK DLLVFCGVAI GGTWMMFQSF KDGMADAVRH QGKGKRQRQK LRYRQARDNK
VGIEVYGDDA TMEHYFGAAY TEKGKKSGKT KGMGTKNRRF VNMYGYNPED FSFIRFLDPL
TGKTMDEQVF SDISLVQDAF SKERLKLLSE GEIESEHMRN GIRAYLVKNL TTAALEIDMT
PHNSCQLGAK TNNIAGYVDR EYELRQTGEA RVVAPALIPK DNPITDEDIP VKHESKTLFR
GLRDYNPIAA AICLLTNESD GMKETMYGIG FGNTIITNQH LFRRNNGVLR VQSRHGEYVL
PNTTQLKVLP CEGRDIMVII LTPDFPPFPQ KLKFRPPIKG EKICLVGSLF QDKSITSTVS
ETSVTTPVDN SFLWKHWITT KDGHCGLPLV SSNDGYIVGI HSATSSRQTQ NYHAAMPEDF
HQTHLIDPAS KSWVKHWKYN PDNMVWGGIN LINSTPREPF KINKLVTDLF GDAVQFQSKQ
DEWFASQLKG NLKAVGKSTS QLVTKHTVKG KCMMFELYLQ THEEEKEFFK PLMGAYQKSR
LNREAFTKDI MKYSTPITVG IVDCDTFLKA EEGVIKRLER LGFSGCEYVT DEEAIFQALN
MKAAVGALYS GKKRDYFEGY GPEEKENILR ESCKRLYTGK FGVWNGSLKS ELRPMEKVMA
NKTRVFTAAP LDTLLAGKVC VDDFNNYFYS KNIEAPWTVG MTKFYGGWNE LLTKLPDGWV
YCDADGSQFD SSLSPFLINS VLRIRLKFME DWDLGEQMLK NLYTEIVYTA ILTPDSTIVK
KFKGNNSGQP STVVDNTLMV VLAMTYTLHK LGFEDEEQDS MCKYFVNGDD LIIAIKPEHE
SLLDQFQHCF KSLGLNYDFN SRTRKKEELW FMSHCGIKKD GIFIPKLEPE RIVSILEWDR
SDQPVHRLEA ICAAMIESWG YDKLTHEIRK FYKWCLEQAP YADLAKAGKA PYIAECALKR
LYTSKEASEA ELEKYMEAIR SLVNDEDDDD MDEVYHQVDA KLDAGQGSKT DDKQKNSADP
KDNIITEKGS GSGQMKKDDD INAGLHGKHT IPRTKAITQK MKLPMIRGKV ALNLDHLLEY
EPNQRDISNT RATQKQYESW YDGVKNDYDV DDSGMQLILN GLMVWCIENG TSPNINGTWV
MMDGEEQVEY ALKPIIEHAK PTFRQIMAHF SDAAEAYIEM RNKKKPYMPR YGRLRGLNDM
GLARYAFDFY ETTSATPNRA REAHNQMKAA ALVGTQNRLF GMDGGGSTQE ENTERHTAAD
VNQNMHTLLG VRGLH
