POLG_PVMA
ID POLG_PVMA Reviewed; 3059 AA.
AC Q85197;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Potato virus A (PVA).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12215;
OH NCBI_TaxID=45843; Solanum betaceum (Tamarillo) (Cyphomandra betacea).
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8113771; DOI=10.1099/0022-1317-75-2-457;
RA Puurand U., Makinen K., Paulin L., Saarma M.;
RT "The nucleotide sequence of potato virus A genomic RNA and its sequence
RT similarities with otherpotyviruses.";
RL J. Gen. Virol. 75:457-461(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2667-3059.
RX PubMed=1604933; DOI=10.1016/0168-1702(92)90070-p;
RA Puurand U., Mkinen K., Baumann M., Saarma M.;
RT "Nucleotide sequence of the 3'-terminal region of potato virus A RNA.";
RL Virus Res. 23:99-105(1992).
RN [3]
RP PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX PubMed=11961277; DOI=10.1099/0022-1317-83-5-1211;
RA Merits A., Rajamaeki M.-L., Lindholm P., Runeberg-Roos P., Kekarainen T.,
RA Puustinen P., Maekelaeinen K., Valkonen J.P.T., Saarma M.;
RT "Proteolytic processing of potyviral proteins and polyprotein processing
RT intermediates in insect and plant cells.";
RL J. Gen. Virol. 83:1211-1221(2002).
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).
RN [5]
RP COVALENT RNA LINKAGE (VIRAL GENOME-LINKED PROTEIN), AND URIDYLYLATION
RP (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=15218030; DOI=10.1074/jbc.m402910200;
RA Puustinen P., Makinen K.;
RT "Uridylylation of the potyvirus VPg by viral replicase NIb correlates with
RT the nucleotide binding capacity of VPg.";
RL J. Biol. Chem. 279:38103-38110(2004).
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=Q85197-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK05-1; 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. {ECO:0000269|PubMed:15218030}.
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: 6K1 and 6K2 are involved in infectivity, as their
CC deletion renders PVA non-infectious.
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; Z21670; CAA79766.1; -; Genomic_RNA.
DR MEROPS; C04.014; -.
DR MEROPS; C06.001; -.
DR Proteomes; UP000008484; 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 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..3059
FT /note="Genome polyprotein"
FT /id="PRO_0000420014"
FT CHAIN 1..298
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040385"
FT CHAIN 299..755
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040386"
FT CHAIN 756..1102
FT /note="Protein P3"
FT /id="PRO_0000040387"
FT CHAIN 1103..1154
FT /note="6 kDa protein 1"
FT /id="PRO_0000040388"
FT CHAIN 1155..1789
FT /note="Cytoplasmic inclusion protein"
FT /id="PRO_0000040389"
FT CHAIN 1790..1842
FT /note="6 kDa protein 2"
FT /id="PRO_0000040390"
FT CHAIN 1843..2031
FT /note="Viral genome-linked protein"
FT /id="PRO_0000040391"
FT CHAIN 2032..2274
FT /note="Nuclear inclusion protein A"
FT /id="PRO_0000040392"
FT CHAIN 2275..2790
FT /note="Nuclear inclusion protein B"
FT /id="PRO_0000040393"
FT CHAIN 2791..3059
FT /note="Capsid protein"
FT /id="PRO_0000040394"
FT DOMAIN 154..298
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 633..755
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1226..1378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1397..1556
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2032..2250
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2516..2640
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT MOTIF 349..352
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 607..609
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1328..1331
FT /note="DEFH box"
FT MOTIF 1883..1890
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 207
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 216
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 249
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 641
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 714
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2077
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2112
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2182
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1239..1246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 298..299
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 755..756
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1102..1103
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1154..1155
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1789..1790
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 2031..2032
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2274..2275
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2790..2791
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1905
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3059 AA; 346080 MW; EFE897679595693A CRC64;
MATQVIMVGE FKILEVNCKP HAPVAAIHVP TQTPKTNDIK WADLEFTLAK SLQRQAHGVV
KVDKHGTARI KRASKHHMSC LEQQMADEVA EKEAFMAAPT QLVTSIIFAG TTPPSMMETE
TIVKKIHTVG KRAKVMRKRS YITPPTDKSL RNHGVTPYSV QQLCRTLGNL SKRTGISLEV
VGKTSKATKL RFTKTSFGHM ARVQLKHHDG RMHRRDLVVD TSTTTIMQTL FLKTARTNAN
LDVLTHGSSG LVFWNYLVTG QRMRTRDNFI IVRGRCNGIL VDARAKLSES TMLSTHHYST
GDVFWRGFNR TFLENKPINL DHVCSSDFSV EECGSIAALI CQSLLPCGKI TCRACAAKNL
NMDEDTFKEF QTQRAREISA VIISEHPNFA CVSQFIDRYF SHQRVLNPNV NAYREILKIV
GGFTQSPYTH IQELNEILVL GGRATPEQLG SASAHLLEIT RFVRNRTDNI KKGSLALFRN
KISAKAHVNT ALMCDNQLDR NGNLIWGERG YHAKRFFSNY FDIITPGGGY KQYIERRVPN
GIRKLAIGNL IVTTNLEALR EQLEGESIEK KAVTKACVSM SDNNYKYPCC CVTLDDGTPL
YSTFIMPTKN HLVIGNSGDP KFLDLPADIS TQMYIAKSGY CYINIFLAML VNVDESDAKD
FTKKVRDIIV PDLGEWPTLI DVATSCSLLS AFYPATSAAE LPRILVDHDL KTMHVIDSYG
SLNTGYHVLK ANTIRQLIQF ASNSLDSEMK HYRVGGTSNS QINGYATIKM LAKAVYRPKL
MKEIIHEQPF MLVMSLMSPG ILIALANSGA LEMGIHHWIR EGDSLVKMAH MLRTVAQNVS
VARATWVQQE IISDSAQQML ETILNGTIPN VSYFQAIQYL TMLAASKEVD AEVRVTGYYT
FKLQTSELLE KTYLSLLEDS WQELSYFGRF QAIRHSRRYC TAGTIVVKPE RHVDLGGIYA
TSYQFALAKQ MEYSKKAVCQ AVNGLQARFN NITSQIYCKI LNWPKRLFPD LVKFINTMLA
ITVALQLYIA FATILRHHQQ CKQDSLELEY CKKERQLITL YDFFIAKQPY ATEEEFMAHV
DEQNPDLSNF AREYCAEVVL FQAKASEQVN FERIIAFISL VLMMFDRERS DCVYRSLTKL
KSLMSTVENT VQFQSLDDIG PTLEEKNMTI DFDLDTDTIV GKSIIGHTFK EWWDVQLNTN
RIVPHYRTEG HFMEFTRANA PTIAHQIAHD LHTDIMLRGA VGSGKSTGLP YHLSKKGTVL
LLEPTRPLAE NVTKQLKSDP FHVSPTLRMR GMAVFGSTPI HVMTTGFALH YLANNLKMLS
TYDFIIIDEF HVHDSNAIAL RNLLHEHNYQ GKLIKVSATP PGREVEFSTQ YPVEIRVEDQ
VSFQDFVKAQ GNGSNLDLTS KCDNLLVYVA SYNEVDQLSK LLLERHFLVT KVDGRSMKLG
QVEIITKGSA NKKHFIVATN IIENGVTLDI DAVIDFGMKV VPFLDSDNRM ISYNKVSISY
GERIQRLGRV GRNKAGVALR IGHTEKGISD VPVVIATQAA FLGFVYGLPI STQSVTTQVL
SNVTLKQART MVQFELPIFY MAHLVRYDGT MHPAIHNELK KYKLRDSEIQ LRKLAIPSKC
VPIWMTGKAY RLLTHNSQIP DDVRVPFLTK EIPDKLHENV WAIVEKFKCD AGIGRMTSAQ
ASKVAYTLET DIHSVQRTIL IIDQLLEREM QKQSHFEMVT NQSCSSGMLS LQTMMNAIQS
RYAKNHTAGN IEILQRAKAQ LLEFSNLSGD ISTESALREF GYLEAVQFQS GTQVSNFLGL
EGHWKKSLIT KDLLIVGGVC VGAAWMIGEY FFKKSKGVVA FQGIISDRGK KLKFARARDE
KMGHYVEAPD STLEHYFGSA YTKKGKTKGK THGMGKKNHR FVNMYGFDPS DYTFIRYVDP
LTGYTLDESP YTDIRLIQSQ FSDIREQQLL NDELERNMVH YKPGVQGYLV KDKTSQILKI
DLTPHIPLKV CDATNNIAGH PDREGELRQT GKGQLLDYAE LPQKKESVEF ESTSMFRGVR
DYNPISSVIC QLENESEGRT TQLFGLGFGP FIITNQHLFV RNNGSLTVRS QMGVFKVNST
VALQMRPVEG RDVLIIKMPK DFPPFPQRLK FRQPTHSEKV CLILTNFQQK SSSSMVSETS
ILYQRKNTYF WKHWISTKEG HCGSPIVSTT DGAILGIHSL SNMTNTSNYF ACFPKGFTET
YLATESVHEW VKGWKFNANN VCWGSFHLQD SKPTKEFKTV KLVTDLLGEA VYTQGCDSKW
LFNAAHTNIQ AVAQLESNLV TKHTVKGKCK LFETYLNVDK AAHDFFSKYM GFYKPSKLNR
EAYTQDLMKY SKVIQVGEVD CGVFESALTG LLHNLGRWGF TTACYTTDED SIYTALNMKA
AVGALYRGKK RDYFDAMSPS EREHLLFLSC KRLYFGQLGV WNGSLKAELR PKEKVDLNKT
RTFTAAPIET LLGGKVCVDD FNNMFYSLHL KAPWSVGMTK FYGTWNQLMC KLPDDWVYCD
ADGSQFDSSI SPYMINAVLR IRLHFMEDWD IGSQMLQNLY TEIGTHQSQH QMAQLLKKFK
GNNSGQPSTV VDNTLLVVLA LHYALLKSGI PLEEQDSVCA YGVNGDDLLI AIRPDMEHKL
DGFQALFSEL GLNYEFNSRS KDKKDLWFMS HKAIQCGEIL IPKLEEERIV SILEWDRSHE
PIHRLEAICA SMVESWGYPE LTHEIRRFYA WVLEQSPYNA LATTGLAPYI AESALKTLYT
NVHPTSTELE KYSIQFDEQM DEEDDMVYFQ AETLDASEAL AQKSEGRKKE RESNSSKAVA
VKDKDVDLGT AGTHSVPRLK SMTSKLTLPM LKGKSVVNLD HLLSYKPKQV DLSNARATHE
QFQNWYDGVM ASYELEESSM EIILNGFMVW CIENGTSPDI NGVWTMMDNE EQVSYPLKPM
LDHAKPSLRQ IMRHFSALAE AYIEMRSREK PYMPRYGLQR NLRDQSLARY AFDFYEITAT
TPIRAKEAHL QMKAAALKNS NTNMFGLDGN VTTSEEDTER HTATDVNRNM HHLLGVKGV
