POLG_SBMVN
ID POLG_SBMVN Reviewed; 3066 AA.
AC P21231;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
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 Soybean mosaic virus (strain N) (SMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12223;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Eggenberger A.L., Beachy R.N., Hill J.H.;
RT "Two genes of soybean mosaic virus are involved in the interaction with the
RT Rsv1 resistance allele of soybean.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2764-3066, AND PROTEIN SEQUENCE OF
RP 2845-2859.
RX PubMed=2661723; DOI=10.1099/0022-1317-70-7-1853;
RA Eggenberger A.L., Stark D.M., Beachy R.N.;
RT "The nucleotide sequence of a soybean mosaic virus coat protein-coding
RT region and its expression in Escherichia coli, Agrobacterium tumefaciens
RT and tobacco callus.";
RL J. Gen. Virol. 70:1853-1860(1989).
RN [3]
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 [4]
RP INTERACTION WITH HOST PLANT EIF4E1 (VIRAL GENOME-LINKED PROTEIN),
RP INTERACTION WITH HOST PLANT EIF4E1 (NUCLEAR INCLUSION PROTEIN A),
RP INTERACTION WITH HOST PLANT EIF4E1 (NUCLEAR INCLUSION PROTEIN B),
RP SUBCELLULAR LOCATION (VIRAL GENOME-LINKED PROTEIN), SUBCELLULAR LOCATION
RP (NUCLEAR INCLUSION PROTEIN A), AND SUBCELLULAR LOCATION (NUCLEAR INCLUSION
RP PROTEIN B).
RC STRAIN=SC3/7/15/18, and SMV-R;
RX PubMed=31860775; DOI=10.1111/mpp.12897;
RA Gao L., Luo J., Ding X., Wang T., Hu T., Song P., Zhai R., Zhang H.,
RA Zhang K., Li K., Zhi H.;
RT "Soybean RNA interference lines silenced for eIF4E show broad potyvirus
RT resistance.";
RL Mol. Plant Pathol. 21:303-317(2020).
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 -!- SUBUNIT: [Nuclear inclusion protein A]: Interacts with host eIF4E
CC proteins in the host cytoplasm. {ECO:0000269|PubMed:31860775}.
CC -!- SUBUNIT: [Nuclear inclusion protein B]: Interacts with host eIF4E
CC proteins in the host cytoplasm. {ECO:0000269|PubMed:31860775}.
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: [Nuclear inclusion protein A]: Host cytoplasm
CC {ECO:0000269|PubMed:31860775}. Note=Binds to host plant eIF4E proteins
CC in the host cytoplasm. {ECO:0000269|PubMed:31860775}.
CC -!- SUBCELLULAR LOCATION: [Nuclear inclusion protein B]: Host cytoplasm
CC {ECO:0000269|PubMed:31860775}. Note=Binds to host plant eIF4E proteins
CC in the host cytoplasm. {ECO:0000269|PubMed:31860775}.
CC -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000269|PubMed:31860775}. Note=Binds to host plant eIF4E proteins
CC in the host nucleus. {ECO:0000269|PubMed:31860775}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P21231-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK08-1; 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; D00507; BAA00398.2; -; Genomic_RNA.
DR PIR; PS0081; PS0081.
DR RefSeq; NP_072165.1; NC_002634.1.
DR GeneID; 918483; -.
DR KEGG; vg:918483; -.
DR Proteomes; UP000007016; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA: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; IPR011492; DEAD_Flavivir.
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; PF07652; Flavi_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 Direct protein sequencing; Helical capsid protein; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host nucleus;
KW Host-virus interaction; Hydrolase; 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 RNA replication; Virion.
FT CHAIN 1..3066
FT /note="Genome polyprotein"
FT /id="PRO_0000420023"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040438"
FT CHAIN 309..765
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040439"
FT CHAIN 766..1112
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040440"
FT CHAIN 1113..1164
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040441"
FT CHAIN 1165..1798
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040442"
FT CHAIN 1799..1851
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040443"
FT CHAIN 1852..2041
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040444"
FT CHAIN 2042..2284
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040445"
FT CHAIN 2285..2801
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040446"
FT CHAIN 2802..3066
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040447"
FT DOMAIN 168..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 643..765
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1236..1388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1407..1566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2042..2260
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2526..2650
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2799..2836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..364
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 617..619
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1338..1341
FT /note="DECH box"
FT MOTIF 1891..1900
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2799..2820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2821..2835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 230
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 262
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 651
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 724
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2087
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2122
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2192
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1249..1256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 308..309
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 765..766
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1112..1113
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1164..1165
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1798..1799
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1851..1852
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2041..2042
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2284..2285
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2801..2802
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1915
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT CONFLICT 2764
FT /note="A -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3066 AA; 349846 MW; 394149153DD5328F CRC64;
MATIMIGSMA ISVPNTHVSC ASNSVMPVQA VQMAKQVPSA RGVLYTLKRE GSTQVHKHEE
ALRKFQEAFD QDVGIQRRLL VNKHSSIQST KKNGLTLRRL TLEQARAKEA AIARRKQEEE
DFLNGKYEQQ FYAGVSATKS MKFEGGSVGF RTKYWRPTPK KTKERRATSQ CRKPTYVLEE
VLSIASKSGK LVEFITGKGK RVKVCYVRKH GAILPKFSLP HEEGKYIHQE LQYASTYEFL
PYICMFAKYK SINADDITYG DSGLLFDERS SLTTNHTKLP YFVVRGRRNG KLVNALEVVE
NMEDIQHYSQ NPEAQFFRGW KKVFDKMPPH VENHECTTDF TNEQCGELAA AISQSIFPVK
KLSCKQCRQH IKHLSWEEYK QFLLAHMGCH GPEWETFQEI DGMRYVKRVI ETSTAENASL
QTSLEIVRLT QNYKSTHMLQ IQDINKALMK GPSVTQSELE QASKQLLAMT QWWKNHMTLT
DEDALKVFRN KRSSKALLNP SLLCDNQLDK NGNFVWGERG RHSKRFFANY FEEVVPSEGY
SKYVIRKNPN GQRELAIGSL IVPLDFERAR MALQGKSVTR EPITMSCISR QDGNFVYPCC
CVTHDDGKAF YSELRSPTKR HLVIGTSGDP KYIDLPATDA DRMYIAKEGF CYLNIFLAML
VNVNEDEAKD FTKMVRDVIV PRLGKWPTML DVATAAYMLT VFHPETRNAE LPRILVDHAC
QTMHVIDSFG SLTVGYHVLK AGTVNQLIQF ASNDLQSEMK FYRVGGEVQQ RMKCETALIT
SIFKPKRMIQ ILENDPYILL MGLVSPSILI HMYRMKHFEK GVELWISKEH SVAKIFIILE
QLTKRVAAND VLLEQLEMIS ETSERFMSIL EDCPQAPHSY KTAKDLLTMY IERKASNNQL
VENGFVDMND KLYMAYEKIY SDRLKQEWRA LSWLEKFSIT WQLKRFAPHT EKCLTKKVVE
ESSASSGNFA SVCFMNAQSH LRNVRNTLFQ KCDQVWTASV RAFVKLIIST LHRCYSDIVY
LVNICIIFSL LVQMTSVLQG IVNTVRRDKA LLSGWKRKED EEAVIHLYEM CEKMEGGHPS
IEKFLDHVKG VRPDLLPVAV SMTGQSEDVS AQAKTATQLQ LEKIVAFMAL LTMCIDNERS
DAVFKVLSKL KAFFSTMGED VKVQSLDEIQ SIDEDKKLTI DFDLETNKES SSVSFDVKFE
AWWNRQLEQN RVIPHYRSTG EFLEFTRETA AKIANLVATS SHTEFLIRGA VGSGKSTGLP
HHLSKKGKVL LLEPTRPLAE NVSKQLSFEP FYHNVTLRMR GMSKFGSSNI VVMTSGFAFH
YYVNNPQQLS DFDFIIIDEC HVQDSPTIAF NCALKEFEFS GKLIKVSATP PGRECEFTTQ
HPVKLKVEDH LSFQNFVQAQ GTGSNADMIQ HGNNLLVYVA SYNEVDQLSR LLTEKHYKVT
KVDGRTMQMG NVEIATTGTE GKPHFIVATN IIENGVTLDI DCVIDFGLKV VATLDTDNRC
VRYNKQSVSY GERIQRLGRV GRCKPGFALR IGHTGKGVEE VPEFIATEAA FLSFAYGLPV
TTQSVSTNIL SRCTVKQARV ALNFELTPFF TTNFIKYDGS MHPEIHRLLK SYKLRESEML
LTKIAIPYQF VGQWVTVKEY ERQGIHLNCP EKVKIPFYVH GIPDKLYEML WDTVCKYKND
AGFGSVKSVN ATKISYTLST DPTAIPRTLA ILDHLLSEEM TKKSHFDTIG SAVTGYSFSL
AGIADGFRKR YLKDYTQHNI AVLQQAKAQL LEFDCNKVDI NNLHNVEGIG ILNAVQLQSK
HEVSKFLQLK GKWDGKKFMN DAVVAIFTLV GGGWMLWDYF TRVIREPVST QGKKRQIQKL
KFRDAFDRKI GREVYADDYT MEHTFGEAYT KKGKQKGSTR TKGMGRKSRN FIHLYGVEPE
NYSMIRFVDP LTGHTMDEHP RVDIRMVQQE FEEIRKDMIG EGELDRQRVY HNPGLQAYFI
GKNTEEALKV DLTPHRPTLL CQNSNAIAGF PEREDELRQT GLPQVVSKSD VPRAKERVEM
ESKSVYKGLR DYSGISTLIC QLTNSSDGHK ETMFGVGYGS FIITNGHLFR RNNGMLTVKT
WHGEFVIHNT TQLKIHFIQG KDVILIRMPK DFPPFGKRNL FRQPKREERV CMVGTNFQEK
SLRATVSESS MILPEGKGSF WIHWITTQDG FCGLPLVSVN DGHIVGIHGL TSNDSEKNFF
VPLTDGFEKE YLENADNLSW DKHWFWEPSK IAWGSLNLVE EQPKEEFKIS KLVSDLFGNT
VTVQGRKERW VLDAMEGNLA ACGQADSALV TKHVVKGKCP YFAQYLSVNQ EAKSFFEPLM
GAYQPSRLNK DAFKRDFFKY NKPVVLNEVD FQSFERAVAG VKLMMMEFDF KECVYVTDPD
EIYDSLNMKA AVGAQYKGKK QDYFSGMDSF DKERLLYLSC ERLFYGEKGV WNGSLKAELR
PIEKVQANKT RTFTAAPIDT LLGAKVCVDD FNNQFYSLNL TCPWTVGMTK FYRGWDKLMR
SLPDGWVYCH ADGSQFDSSL TPLLLNAVLD VRSFFMEDWW VGREMLENLY AEIVYTPILA
PDGTIFKKFR GNNSGQPSTV VDNTLMVVIA MYYSCCKQGW SEEDIQERLV FFANGDDIIL
AVSDKDTWLY DTLSTSFAEL GLNYNFEERT KKREELWFMS HKAVLVDGIY IPKLEPERIV
SILEWDRSKE LMHRTEAICA SMIEAWGYTE LLQEIRKFYL WLLNKDEFKE LASSGKAPYI
AETALRKLYT DVNAQTSELQ RYLEVLDFNH ADDCCESVSL QSGKEKEGDM DADKDPKKST
SSSKGAGTSS KDVNVGSKGK VVPRLQKITR KMNLPMVEGK IILSLDHLLE YKPNQVDLFN
TRATRTQFEA WYNAVKDEYE LDDEQMGVVM NGFMVWCIDN GTSPDANGVW VMMDGEEQIE
YPLKPIVENA KPTLRQIMHH FSDAAEAYIE MRNSESPYMP RYGLLRNLRD RELARYAFDF
YEVTSKTPNR AREAIAQMKA AALSGVNNKL FGLDGNISTN SENTERHTAR DVNQNMHTLL
GMGPPQ
