POLG_PEMVC
ID POLG_PEMVC Reviewed; 3068 AA.
AC Q01500;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Pepper mottle virus (isolate California) (PeMV) (PepMoV C).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=31737;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=4075; Datura inoxia (Downy thornapple) (Datura meteloides).
OH NCBI_TaxID=4107; Solanum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1413501; DOI=10.1016/0042-6822(92)90162-i;
RA Vance V.B., Moore D., Turpen T.H., Bracker A., Hollowell V.C.;
RT "The complete nucleotide sequence of pepper mottle virus genomic RNA:
RT comparison of the encoded polyprotein with those of other sequenced
RT potyviruses.";
RL Virology 191:19-30(1992).
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 TOMATO EIF4E1 (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=22242134; DOI=10.1371/journal.pone.0029595;
RA Mazier M., Flamain F., Nicolai M., Sarnette V., Caranta C.;
RT "Knock-down of both eIF4E1 and eIF4E2 genes confers broad-spectrum
RT resistance against potyviruses in tomato.";
RL PLoS ONE 6:e29595-e29595(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=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 (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:22242134}.
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=Q01500-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK01-1; 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; M96425; AAA46903.1; -; Genomic_RNA.
DR PIR; A44062; A44062.
DR RefSeq; NP_041276.1; NC_001517.1.
DR MEROPS; C04.002; -.
DR MEROPS; C06.001; -.
DR PRIDE; Q01500; -.
DR GeneID; 1494047; -.
DR KEGG; vg:1494047; -.
DR Proteomes; UP000008157; 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; IDA: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 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; 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..3068
FT /note="Genome polyprotein"
FT /id="PRO_0000420003"
FT CHAIN 1..287
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040295"
FT CHAIN 288..743
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040296"
FT CHAIN 744..1104
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040297"
FT CHAIN 1105..1156
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040298"
FT CHAIN 1157..1790
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040299"
FT CHAIN 1791..1842
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040300"
FT CHAIN 1843..2030
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040301"
FT CHAIN 2031..2276
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040302"
FT CHAIN 2277..2795
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040303"
FT CHAIN 2796..3068
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040304"
FT DOMAIN 144..287
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 621..743
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1228..1380
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1399..1558
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2031..2249
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2518..2642
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2796..2833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 337..340
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 595..597
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1330..1333
FT /note="DECH box"
FT MOTIF 1884..1891
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2797..2832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 204
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 238
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 629
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 702
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2076
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2111
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2181
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1241..1248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 287..288
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 743..744
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1104..1105
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1156..1157
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1790..1791
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1842..1843
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2030..2031
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2276..2277
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2795..2796
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1906
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3068 AA; 348656 MW; FD3458B837FDA7C2 CRC64;
MATSVIQFGS FVCNLPKSQP LCTTVHCPKQ SMSTNIVRPS DPFAELEKHL EPYLQKRMDA
TIRQTKGGTL VYKHMSEAKR ARKLRKKQRE EEEVRLFMNA APYIVSNITI GGGEVPSKME
EVSIKRPLNK TPSRKIKKSL TPVTFRDGHM NKFLRELRDC ATRNSMTVHL IGKRKTELAF
KRRASLNAVY ATLHHMRGVD RKRDIVLEEW MNDYVLNLSK VSTWGSLFHA ESLKRGDSGL
ILNARALRGK FGRCSRGFFI VRGKSDGVVL DARSKLSMAT VTHMEQYSTP EAFWSGLEKK
WSVVRKPTAH TCKPTYSVSN CGEVAAIIAQ ALFPCHKLTC GECSKEICDL TSNECVQELY
KNTSLALERM NNLHPEFQHI VKVLSVVRQL TEASNHGTET FDEIFKMIGS KTQSPFTHLN
KLNEFMLKGN ENTSGEWLTA RQHLRELVRF QKNRTDNIKK GDLASFRNKL SARAQYNLYL
SCDNQLDKNA SFLWGQREYH ARRFFLNFFQ QIDPSKGYLA YEDRTIPNGS RKLAIGNLIV
PLDLAEFRKR MNGIDTQQPP IGKYCTSQLD GNFVYPCCCT TLDDGQPIRS AVYAPTKKHL
VVGNTGDTKY INLPKGDTEM LYIALDGYCY INIYLAMLVN ISEEEAKDFT KKVRDIFMPK
LGKWPTLMDL ATTCAQLRIF HPDVHDAELP RILVDHNTQT CHVVDSYGSI STGYHILKAA
TVSQLVLFAD DNLESEIKHY RVGGIVENHK VQIDNQPSRC GVSEFHAIRM LIKGIYRPSV
MYELLSEEPY LLVFSILSPS ILIAMYNDRA FELAVQIWLE KEQSIPLIAT ILTNLAAKVS
VATTLVQQLQ LIELSADQLL NVTCDGFRVS FAYQSALTLL TRMRDQAKAN SELISGGFNE
YDQDLAWTLE KNYQGLLHDQ WKELSSLEKF RYYWSSRKRK TRLRSNIKSR SSPVASAISS
LSLKPFMGKV FSHMKAGAVC TKQGTKNFID ARCLGISTYF VGSLMRKFPS AKVLLSSLFV
LGALLNITHA ANRIIIDNRI SREHAAALEL YRKEDTCHEL YTALERKLGE KPTWDEYCSY
VAKINPAMLE FIKDSYDEKQ VVHQRSTEDL KKVEHIIAFV TLAIMLFDSE RSDCVFKTLN
KFKGVVCSLG SGVRHQSLDD FVSTMDEKNF VVDFELNDSV QRKNLTTEIT FESWWDEQVA
RGFTIPHYRT EGRFMEFTRA TAAKVASDIS ISSERDFLIR GAVGSGKSTG LPHHLSTYGR
VLLIEPTRPL AENVFKQLSG GPFFLKPTMR MRGNSVFGSS PISVMTSGFA LHFFANNITQ
LQEIQFIIID ECHVMDASSM AFRSLIHTYH TNCKVLKVSA TPPGREVEFT TQFPVKLVVE
DSLSFKTFVE SQGTGSNCDM IQYGNNLLVY VASYNEVDQL SKLLVAREFN VTKVDGRTMK
HGELEIVTRG TKSKPHFVVA TNIIENGVTL DIDVVIDFGM KVSPFLDVDN RSVAYNKVSI
SYGERIQRLG RVGRIQKGTA LRIGHTEKGL IEIPQMISTE AALYCFAYNL PVMSSGVSTS
MIKNCTIPQV RTMHTFELSP FFMYNFVSHD GTMHPVVHET LKRYKLRDSV IPLSESSIPY
RASSDWITAG DYRRIGVKLD IPDETRIAFH IKTFHRKFTN NLWESVLKYK ASAAFPTLRS
SSITKIAYTL STDLYAIPRT LAVVESLLED ERTKQYQFKS LIDNGCSSMF SVVGISNALR
AKYSKDHTVE NINKLETVKA QLKEFHNLNG SGDELNLIKR FESLQFVHHQ SKSSLAKALG
LRGVWNKSLI VRDAIIAAGV ACGGAWLLYT WFTAKMSEVS HQGRSKTKRI QALKFRKARD
KRAGFEIDNN EDTIEEYFGS AYTKKGKGKG TTVGMGRTNR RFINMYGFEP GQFSYIKFVD
PLTGAQMEEN VYADIVDVQE KFGDIRRQMI LDDELDRRQT DVHNTIHAYL IKDWSNKALK
VDLTPHNPLR VSDKASAIMK FPEREGELRQ TGQAVEVDVC DIPKEVVKHE AKTLMRGLRD
YNPIAQTVCK LTVKSELGET STYGLGFGGL IIANHHLFKS FNGSLEVKSH HGVFRVPNLM
AISVLPLKGR DMIIIKMPKD FPVFPQRLKF REPASTDRVC LIGSNFQERY ISTTVSEISA
THPVPRSTFW KHWISTDDGH CGLPIVSTTD GFILGLHSLA NNRNSENYYT AFDSDFEMKI
LRSGENTEWV KNWKYNPDTV LWGPLQLTKG TPSGMFKTTK MIEDLLAFKS ESVREQAHTS
SWMLEVLKEN LKAIAYMKSQ LVTKHVVKGE CMMFKQYLQE NPRANEFFQP KMWAYGKSML
NKEAYIKDIM KYSKVIDVGV VDCDRHLRKL SLELLYTQIH GFRKCSYITD EEEIFKALNI
TTAVGAMYGG KKKEYFEKFT TEDKAEILRQ SCLRLYTGKL GVWEWALKAE LRSKEKIEAN
KTRTFTAAPI DTLLGGKVCV DDLNNQFYSK NIECCWTVGM TKFYGGWDKL LTALPAGWIY
CDADGSQFDS SLTPYLINAV LTIRYAFMED WDIGYKMLQN LYTEIIYTPI STPDGTIVKK
FRGNNSGQPS TVVDNSLMVV LAMHYAFVRE GIAFEEIDSI CKFFVNGDDL LIAVNPERES
LLDTLSNHFS DLGLNYDFSS RTRNKSELWF MSHCGISVEG TYIPKLEEER IVSILQWDRA
ELPEYRLEAI CAAMIESWGY PQLTHEIRRF YSWLIEKNPY ADLASEGKAP YISELALKKL
YLNQDVQMMS FRSYLKYFAD ADEEFECGTY EVRHQSSSRS DTLDAGEEKK KNKEVATVSD
GMGKKEVEST RDSDVNAGTV GTFTIPRIKS ITEKMRMPKQ KRKGVLNLAH LLEYKPSQVD
ISNTRSTQAQ FDNWYCEVMK AYDLQEEAMG TVMNGLMVWC IENGTSPNIS GTWTMMDGDE
QVEFPLKPVI ENAKPTFRQI MAHFSDVAEA YIEMRNKQEP YMPRYGLVRN LRDMGLARYA
FDFYEVTSRT STRAREAHIQ MKAAALKSAQ TRLFGLDGGI GTQGENTERH TTEDVSPDMH
TLLGVREM
