ID   POLG_PSBMV              Reviewed;        3206 AA.
AC   P29152;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 169.
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   Pea seed-borne mosaic virus (strain DPD1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus; Potyvirus pisumsemenportati;
OC   Pea seed-borne mosaic virus.
OX   NCBI_TaxID=31736;
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea) (Lathyrus oleraceus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1940858; DOI=10.1099/0022-1317-72-11-2625;
RA   Johansen E., Rasmussen O.F., Heide M., Borkhardt B.;
RT   "The complete nucleotide sequence of pea seed-borne mosaic virus RNA.";
RL   J. Gen. Virol. 72:2625-2632(1991).
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).
RN   [3]
RP   INTERACTION WITH HOST EIF4E (VIRAL GENOME-LINKED PROTEIN), AND SUBCELLULAR
RP   LOCATION (VIRAL GENOME-LINKED PROTEIN).
RX   PubMed=21283665; DOI=10.1371/journal.pone.0015873;
RA   Ashby J.A., Stevenson C.E.M., Jarvis G.E., Lawson D.M., Maule A.J.;
RT   "Structure-based mutational analysis of eIF4E in relation to sbm1
RT   resistance to pea seed-borne mosaic virus in pea.";
RL   PLoS ONE 6:e15873-e15873(2011).
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=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:
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 (Probable). 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       ECO:0000305|PubMed:21283665}.
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:0000269|PubMed:21283665}. Note=Binds to host plant eIF4E proteins
CC       in the host nucleus. {ECO:0000269|PubMed:21283665}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P29152-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ99-1; 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; D10930; BAA01726.1; -; mRNA.
DR   PIR; JQ1331; GNVSPV.
DR   RefSeq; NP_056765.1; NC_001671.1.
DR   MEROPS; C04.010; -.
DR   GeneID; 1494045; -.
DR   KEGG; vg:1494045; -.
DR   Proteomes; UP000006689; Segment.
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; EXP: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   1: Evidence at protein 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; Reference proteome;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral immunoevasion; Viral RNA replication; Virion.
FT   CHAIN           1..3206
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420013"
FT   CHAIN           1..397
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040375"
FT   CHAIN           398..856
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040376"
FT   CHAIN           857..1214
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040377"
FT   CHAIN           1215..1266
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040378"
FT   CHAIN           1267..1902
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040379"
FT   CHAIN           1903..1955
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040380"
FT   CHAIN           1956..2149
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040381"
FT   CHAIN           2150..2395
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040382"
FT   CHAIN           2396..2915
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040383"
FT   CHAIN           2916..3206
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040384"
FT   DOMAIN          255..397
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          734..856
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1338..1490
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1494..1668
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2150..2368
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2637..2761
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          2900..2979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           450..453
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           708..710
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1440..1443
FT                   /note="DECH box"
FT   MOTIF           1994..2001
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2916..2939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2949..2974
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        307
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        316
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        348
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        742
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        815
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2195
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2230
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2300
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   BINDING         1351..1358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   SITE            397..398
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            856..857
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1214..1215
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1266..1267
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1902..1903
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1955..1956
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2149..2150
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2395..2396
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2915..2916
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2016
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09814"
SQ   SEQUENCE   3206 AA;  364276 MW;  42A3D921BE9A0CBF CRC64;
     MSTLVCQAVA APVWSNGART RRIRDADGEY RCTQCDMGFD SMTMARPVNH CCDGIMIDEY
     NLYDDDPIMH LVDSKTPIKR GSQETEGDGM AAEAIKVTGA EPVNCFMVGT IKCKINENSI
     VAKGVMAAIP RQLTQDEVFM RKARLQAAVA KSTIEREEKE RQFAFSKLEE KLRARREKLK
     DGIVIKTRKG LEWREATPNQ QRGKLQSTSF DASGGKTLTP HTIYCKTKSS KFSNGGVKCA
     TSKKMRTVRK PQSLKMKTES IDVLIEQVMT IAGKHAKQVT LIDKQKTNRV WIRRVNGVRL
     LQVETKHHKG IISQKDASLN NLTKRVARHF ARKTAYIHPS DSITHGHSGV VFLRANISGS
     KSYSIDDLFV VRGKRNGKLM ESRNKVAWRK MFQIDHFSIV GIKIWNAFDA EYVKLRDESV
     SDHDCVGGIT PEECGILAAQ ILRVFYPCWR ITCTKCISNW LSKPTSEQIE HIYERGNLAI
     QDLNKRIPSA HHVTQMVELL RQRIKNTTFD MGNNTKVHEL IGHRQDGVFR HLNRLNNSIL
     AANGSSTIEW ESMNESLLEL ARWHNKRTES IASGGISSFR NKISAKAQIN FALMCDNQLD
     TNGNFVWGER GYHAKRFFSE FFTKIDPKDG YSHHTVRATP TGVRHLAIGN LIIPGDLQKL
     REKLEGVSIT AVGISEKCVS RRNGDFVYPC SCVTSENGKP VLSDVILPTR NHLVIGNTGD
     PKLVDLPKTE TGRMWIAKEG YCYINIFFAM LVNVSEKDAK DFTKFVRDEI MPQLGKWPTM
     MDVATACYKL AIIYPDVRDA QLPRILVDHS EQIFHVIDSY GSMTTGYHIL KAGTVSQLIS
     FAHGALLGEM KMYRVGGTQK MEINMCCCQR KNLLIKQLIR AIYRPKLLTE IIETEPFVLM
     LAIVSPSILK AMFRSGTFNQ AIKFYMHRSK PTAQTLAFLE ALSERVSRSR VLSEQFNIID
     GALKELKSLA NMSMRTQHTY PIVQNQLDIM IERVSADAEL LRDGFVVSKG RVQALIEKNY
     QDDLRNSFTD LPYVQQLQQT MSFSRVKHGF GELCESKDLS FSKEAWMGHL SSFSAGGKQI
     IRLARTKSQQ MLASGGRRVT LAARNITMRM VTATFSEIMK FVNMLLVLSM IFKLWKQANT
     LLEEREKDKW EKFDRSQNEL RRQLRYTLWR FEAQEGRQVT REEFFDYLKY NEGIENRHEL
     INELIANQPL FSIQAKKHGE IRFEQTVALM ALLAMMFGSD RSDAVFSTLS KVRTIFTTMA
     QEVRCQSIDD IHDVFDEKKA TIDFELATDQ PAQVQMDKTF CEWWQNQMEQ NRTVPHYRTG
     GKFIEFTRSN AASVANEIAH TPDFSEYLIR GAVGSGKSTG LPCYLSAKGR VLLLEPTRPL
     TENVCAQLRG SPFHKSPSMS MRNGHTFGST PIHVMTTGYA LHFFCNNVER IREYDFVIFD
     ECHVIDSSAM SFYCALKEYS YQGKILKVSA TPPGREVEFK TQFPVTIATE DSLSFDQFVQ
     AQGSGANCDI LKKGHNILVY VSSYNEVDRL SKLLVDRGFK VTKVDGRTMK LGGVEINTSG
     TAEKPHFIVA TNIIENGVTL DIDVVVDFGV KVVAELDADA RTMRYNKQAI SYGERIQRLG
     RVGRLKDGHA LRIGHTEKGI TEIPVAIAVE SAFQCFAYGL PVMTSNVSTS IIGNCTVKQA
     RTMMNFELSP FFTVELVKYN GTMHPEIHKI LVPYKLRDSS MQLCKEAIPN SGVSRWHTAH
     EYISHGIVLE TLKSDVRIPF YLKGVPEKVY EKIWNAVCVF KSDSGFGRMS TASACNVAYT
     LKTDPLSITR TIAHIDALLI EEQEKKSQFD LMSSHVTNSS SISLAGLVNR LRSKWMVDHS
     GENIVKLQNA RSQLLEFRGM DINLDDVESF RKFGCAETVR CQSKSEVSKT LQLKGKWNKP
     LITSDFFVVC MVSIGCVVLM YQIFMAKWNE PVKLEGKSKA KTLRFRQARD NNAKYEVFAD
     EDTKRHYFGE AYTKKGKKSG KARGMGVKTK KFVNVYGFDP CEYSLVRFVD PLTGLTYDRH
     PMEHMMDVQE TIGDDRREAM WNDELDKQLF VTRPTIEAYY IKDKTTPALK IDLNPHNPMR
     VCDKAETIAG FPEREFELRQ SGSATLVPYS EVPVQNEKQE FDEEHVRTEA ASLHFGLRDY
     NPIAQAVCRI TNTGVDYDRS IFGIGFGQFL ITNAHCFKLN EGETRIVSRH GQFTIEKTHS
     LPIHQVKDKD MVIVRLPKDF PPFPQRLQFR APQEREKICL VGSNFQEKSI QSVITESCMT
     FKHNGGKYWK HWITTKEGHC GLPAVALKDG HIVGIHNLGG ENTNINYFTP FDADILDKYL
     LNAEALQWTK GWKYNKNKVC WGGLELLDDN EPEESGLFRM VKLLKSLEED GVRTQSRDDA
     WLEKEIKGSL KVVARCPGQL VTKHVVKGPC AMFQLYLELH EDAKSFFTPR MGSYGKSRLS
     KGAFIKDIMK YSSNTVVGNV DCDVFENAID NVEKILWKAG MMQCEYVTDA EAIFQSLNMN
     AAVGAMYQGK KKDYFEDFTA ADRELIVKQS CERLFLGKKG VWNGSLKAEL RPIEKVHENK
     TRTFTAAPLD TLLGGKVCVD DFNNFFYSCH LRGPWTVGIT KFYAGWNEFL SKLPDGWLYC
     DADGSRFDSS LTPYLINAVL ELRLRFMEEW DAGEQMLKNL YTEIIYTPIA TPDGSVIKKT
     KGNNSGQPST VVDNTLMVIL AMQYSLQLLG VDFETQDEVV RYFANGDDLL IAVRPDCEFV
     LKGLEIHFSN LGLNYNFSAR HHDKKDVWFM STRGILRDGI LIPKLEEERI VAILEWDRSR
     EFSHRLDAIC AAMIEAWGYD ELLQHIRKFY YWLLEQEPYR SIAQEGKAPY IAETALRHLY
     TNAMATQSEL EKYTEAINQH YNDEGGDGSI KVRLQAGDET KDDERRRKEE EDRKKREESI
     DASQFGSNRD NKKNKNKESD TPNKLIVKSD RDVDAGSSGT ITVPRLEKIS AKIRMPKHKG
     GVAISLQHLV DYNPAQVDIS NTRATQSQFD NWWRAVSQEY GVGDNEMQVL ASGLMVWCIE
     NGTSPNINGM WTMMDGEEQV EYPLKPVMDN ARPTFRQIMA HFSDVAEAYI EKRNSTEVYI
     PRYALQRNLR DPSLARYGFD FYEITAKTPV RAREAHFQMK AAAIRGKSNS LFGLDGNVGT
     QEENTERHTA EDVNQNMHNL LGMRAM
//