POLG_PEMVM
ID POLG_PEMVM Reviewed; 3099 AA.
AC O56075;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Peanut mottle virus (strain M).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=103926;
OH NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH NCBI_TaxID=108216; Arachis pintoi.
OH NCBI_TaxID=53851; Cassia.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=35627; Stylosanthes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Flasinski S., Gonzales R.A., Cassidy B.G.;
RT "The complete nucleotide sequence of peanut mottle virus (M strain) genomic
RT RNA.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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).
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=O56075-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK00-1; 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; AF023848; AAB94595.1; -; Genomic_RNA.
DR RefSeq; NP_068348.2; NC_002600.1.
DR MEROPS; C06.001; -.
DR PRIDE; O56075; -.
DR GeneID; 912241; -.
DR KEGG; vg:912241; -.
DR Proteomes; UP000000471; 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 3: Inferred from homology;
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..3099
FT /note="Genome polyprotein"
FT /id="PRO_0000420004"
FT CHAIN 1..322
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040305"
FT CHAIN 323..779
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040306"
FT CHAIN 780..1128
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040307"
FT CHAIN 1129..1180
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040308"
FT CHAIN 1181..1814
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040309"
FT CHAIN 1815..1867
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040310"
FT CHAIN 1868..2057
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040311"
FT CHAIN 2058..2303
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040312"
FT CHAIN 2304..2821
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040313"
FT CHAIN 2822..3099
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040314"
FT DOMAIN 180..322
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 657..779
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1252..1404
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1423..1582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2058..2276
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2545..2669
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2831..2869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 374..377
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 631..633
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1354..1357
FT /note="DESH box"
FT MOTIF 1906..1915
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2831..2857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 242
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 275
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 665
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 738
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2103
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2138
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2208
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1265..1272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 322..323
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 779..780
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1128..1129
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1180..1181
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1814..1815
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1867..1868
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2057..2058
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2303..2304
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2821..2822
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1930
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3099 AA; 351038 MW; 0D8E9FC7603F0A4B CRC64;
MASITFGNAC TVVFGQVRKE EVTAGPVAVN LNEGTRMVVV PTAAQMATPT PSVSIKIINR
WSNKAVSSYE RQVEDVFANF FAKKERSDEL LTRYYGKVVQ KGNKLMVKRA PLHVARVLEK
QRLQDIEDEK AFLQYRDAGV HVAGSVKFTD TRSRGQTVSF RTEHYKPTGK IVQKKKAQKQ
RANADVDHLI DEVMKICSAD CKQVEFISMG KRRLTAKFKL FGKSVIPCIH LAHEQGRRLR
RELDPRIHEQ VIAHLVTGRK VRELIKDDMV TYGWSGAILN KNLFKRTPFR WDEVVIRGRL
YGKLVDARSK LSECSKDKIH QYSSFEAQFW KGWKNKFDTL HPHNKDHICE PTINNEKCGE
IVATIFQAIH PVIKVSCSTC RERLTKASNE ELNEYLATNL ACHKATFDDM RQQHATVNTV
LNKIEQTSLA NPNLKDSMEI VRLLQNLNQT QARQLMKVNN TLLKGNVATS EEFSDATTQL
LEVTRWYAKH LSLVDEGSIS SFRNKATSKS LINPSLLCDN QLDRNGNFVW GERGRHSKRF
FENFFEEVVP GGGYKKYQIR NSPNCTRKLA IGNLIVPMSL ERARNALIGE SVERLPVTEA
CVSRVNGAFM HVASCVTSDN GSAHFSPLYS PTKRHLVVGT TGDSKYIDLP ATESDKMYVA
KEGYCYINIF LAMLVNVNED SAKDFTKMIR DTIVPMLGTW PSMMDVATAC YILTVFHPET
KSAELPRILV DHTNKTMHVI DSFGSISTGY HILKAGTVSQ LIHFASNELV SEMKHYVVGG
EAPHARRMRM EKALIQGIFK PKQLVYLIEE DPYILMMSLV SPTLLINLFN VGGLEVAMKH
WIKKEMNIGL IFSMLSSLAQ KVSRADLVNE QITMIDANAA QFIETLAGID VENPMRNELV
SALTMMLARS DVDSTLNKTG FTGFSDTLLE MREKIIGDEL NKVWSELSWW EKFSSIIFSR
RARKHIMAPL PNTKLHAIDD RYAISCTWLH GKIKARFNGA KSATLEVCKK VTSILKRNTV
DSILYICRKC YSDIFYFVNV MLISSMILSV IYTMHKMVIE SRAHKQAMVI MKMREDELVV
KQMYDQYCKL ANETPTKEEF FQYVCKMNKE LGERIAPEFE EGSLVVYQAK TETELGLEKV
VAYLALIAMI FDGERSDAVF RALSKLKTVF GTLGETVRYQ SLDEIESVAD EKKMTIDFEL
EGSEASSSTV MSAKFSDWWY KQLETNRVVP HYRIGGEFVE FTRKTAAEVV NNMRASNASE
FLVRGAVGSG KSTGLPHLLA QKGRVLLLEP TRPLAENVCK QLRQAPFQQN PTLRMRGLTT
FGSSNIVIMT SGFALHYYAN NPTKLQEYDF VMIDESHTMD ASAMAFYCLV REYNFQGKII
KVSATPPGKE CEFKTQFDVA LLIEEDLSFQ QFAQSQGQGG NADMTKHGDN ILVYVASYND
VDQLAELLIR GNHFVTKVDG RTMKMGSTEI VSKGTASKKH YIIATNIIEN GVTLDVDVVV
DFGQKVVAEL DGDSRCMRYR KVAVSYGERI QRLGRVGRVK KGTALRIGHT EHGISEIPAS
ISTEAAFLCF AYGLPVITHN VTVSILANCT VQQARTMMLF ELSPFFLADL VKYNGSMHPE
VHKLLKPYKL RDSEIELCKL AIPNSSIGRW LSVHEYAKLG IKIHAVDSVR IPFAGRGIPD
KLYSELWHII QEHKHEAGFG RLTSASASTI AYTLSTDPEA IPRTIALLDN LIAEEMQKKA
HFEALNSTLC SQRFTLKNIV DTVRQRYMKD HSKHNIEVLQ SARSQILEFN SATHDFKKVA
SLLGYGFLDT VQYQSKNELS KRLGLKGRWN KSLVTNDLLV CGMVLFGGVW MVWEYAKSAM
NEPVRYQGKR QNQKLKFRDA RDRKVGREVY GDDGTIEHFF GEAYTKKGKS KGNHTVKGMG
RKTRRFIHMY GFDPTEYSFV RFVDPLTGYA IDENITCDIS LVQDEVAEVR KQFINEDEIS
AQSIAENPGI IAYYMSRNAD KALKIDLTPH NPLAVGRGGS SIAGFPEREY ELRQTGKPLE
VKKSEVPPVS KDVVATEGKS MCRGLRNYNP IATSICKLVN ESDGHSETIH GIGFGPVIIT
NSHLFRRNNG TLQIQTHHGV FRVKNSTQLQ VSHMAKKDMI IIKMPCDVPP FPSKLRFRQP
EQGEKAVLVG SLFQQKSITS SVSESTMVMP VNDSGYWRHW VSTKDGDCGL PLVSTVDGAI
LGLHGLTSTK SDRNYFVPFD EQFERDILAN LEKLDWKRHW LHSSDLIAWG GMSLKENHPH
DCFRTSKLVT DLLGLTKDSV EYQSGQDKWV LAGLENNLKA VAQSESQLVT KHVVKGQCMY
FQEYLATHST AEKFFKPLMG AYQPSKLNKE AFTKDLYKYQ NEIIVGEVDK DAFDNAVEAV
IYLLDDLGFG ECAYVTDEEA ILDSLNMKAA VGALYKGKKK EYFESLSEPE KHHIVQASCE
RLFYGEMGVW NGSLKAELRP KEKVALNKTR TFTAAPIDTL LGGKCCVDDF NNRFYSLNIE
GPWTVGMTKF YGGWDKLMRK LPDGWRYCHA DGSQFDSSLT PFLLNAVLAV RLMFMEDWWV
GEQMLRNFYT EIIYTPILTP DGTIVKKFKG NNSGQPSTVV DNTLMVMIAM FYGMKKLNWT
DEQIKERIVF FAXGDDLIIA VQPEHEGILD TLQRSLGELG LKYDFSERCD DRQELWFMSH
QGHLVDGMYI PKLEQERIVS ILEWDRSTVI EHRAEAICAA MIEAWGYPEL LKQIRLFYAW
ILDHDMFKSL VAEGKLPYIA ETALRKLYTD ADATDVELEE YILRFTEVDE DEDHNDEVRY
QSGENKSKVE VDAAAAKLKE KEKEKHKKTE EGTSEGTSQT KEPDVDTGSQ GIVYVPKLAK
ITKKMRMPMV GGQVILHIPH LLDYKPEQVD LSNTRSSQQQ FTAWYNGLKE AYEITDDTSM
SVLMNGLMVW CIENGTSPNI NGNWTMMDGH EQNEYPLKPV IENAKPTFRQ IMHHFSDAAE
AYIEMRNAEK PYMPRYGLQR NLRDFSYARI AFDFYEITSR TSAKAREIHM QMKAAALNNV
AIKTFGLDGN VGTQDEDTER HTANDVNRNM HSLLGMRQM
