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   02-SEP-2026, entry version 168.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 protease;
DE              EC=3.4.21.-;
DE     AltName: Full=Leader protease P1;
DE     AltName: Full=N-terminal protein;
DE     AltName: Full=P1 proteinase;
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; Potyvirus lactucae;
OC   Lettuce mosaic virus.
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 russellianum (Showy prairie gentian) (Eustoma grandiflorum).
OH   NCBI_TaxID=4235; Lactuca.
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea) (Lathyrus oleraceus).
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 (By
CC       similarity). Reduces the abundance of host transcripts related to
CC       jasmonic acid biosynthesis therefore altering the host defenses (By
CC       similarity). In order to increase its own stability, decreases host
CC       protein degradation pathways (By similarity).
CC       {ECO:0000250|UniProtKB:P13529, ECO:0000250|UniProtKB:P89509}.
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: [Nuclear inclusion protein B]:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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: [Nuclear inclusion protein A]:
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: [Helper component proteinase]:
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   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; 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 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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.70.150; Helper component proteinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   PANTHER; PTHR43519; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR   PANTHER; PTHR43519:SF1; ATP-DEPENDENT RNA HELICASE HRPB; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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;
KW   Inhibition of host innate immune response by virus; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW   RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW   Thiol protease; Transferase; Viral immunoevasion; Viral RNA replication;
KW   Virion.
FT   CHAIN           1..3255
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000419999"
FT   CHAIN           1..437
FT                   /note="P1 protease"
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        2989..3005
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|UniProtKB:P18247"
FT   SITE            1325..1326
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            1968..1969
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2021..2022
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2214..2215
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2457..2458
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2977..2978
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   MOD_RES         2084
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09814"
FT   MOD_RES         3237
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P17767"
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
//