POLG_ZYMVC
ID POLG_ZYMVC Reviewed; 3080 AA.
AC P18479; Q89334;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Zucchini yellow mosaic virus (strain California) (ZYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117128;
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7844540; DOI=10.1099/0022-1317-76-1-37;
RA Wisler G.C., Purcifull D.E., Hiebert E.;
RT "Characterization of the P1 protein and coding region of the zucchini
RT yellow mosaic virus.";
RL J. Gen. Virol. 76:37-45(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2694-3080.
RX PubMed=2185142; DOI=10.1016/0378-1119(90)90312-f;
RA Gal-On A., Antignus Y., Rosner A., Raccah B.;
RT "Nucleotide sequence of the zucchini yellow mosaic virus capsid-encoding
RT gene and its expression in Escherichia coli.";
RL Gene 87:273-277(1990).
RN [3]
RP FUNCTION (HELPER COMPONENT PROTEINASE), AND MUTAGENESIS OF PRO-618; THR-619
RP AND LYS-620.
RX PubMed=9568986; DOI=10.1099/0022-1317-79-4-897;
RA Peng Y.H., Kadoury D., Gal-On A., Huet H., Wang Y., Raccah B.;
RT "Mutations in the HC-Pro gene of zucchini yellow mosaic potyvirus: effects
RT on aphid transmission and binding to purified virions.";
RL J. Gen. Virol. 79:897-904(1998).
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).
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=P18479-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK13-1; 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; L31350; AAA65559.1; -; Genomic_RNA.
DR EMBL; M35095; AAA48511.1; -; Genomic_RNA.
DR PIR; JH0103; JH0103.
DR MEROPS; C06.001; -.
DR PRIDE; P18479; -.
DR BRENDA; 3.4.22.45; 6761.
DR Proteomes; UP000008610; 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; 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 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..3080
FT /note="Genome polyprotein"
FT /id="PRO_0000420035"
FT CHAIN 1..310
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040500"
FT CHAIN 311..766
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040501"
FT CHAIN 767..1112
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040502"
FT CHAIN 1113..1164
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040503"
FT CHAIN 1165..1798
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040504"
FT CHAIN 1799..1851
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040505"
FT CHAIN 1852..2041
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040506"
FT CHAIN 2042..2284
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040507"
FT CHAIN 2285..2801
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040508"
FT CHAIN 2802..3080
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040509"
FT DOMAIN 170..310
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 644..766
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 2804..2839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..365
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 618..620
FT /note="Involved in virions binding and aphid transmission"
FT MOTIF 1338..1341
FT /note="DECH box"
FT MOTIF 1891..1900
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2812..2829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 232
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 264
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
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 310..311
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255"
FT SITE 766..767
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 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 MUTAGEN 618
FT /note="P->A: Complete loss of aphid transmission and
FT binding to virions."
FT /evidence="ECO:0000269|PubMed:9568986"
FT MUTAGEN 619
FT /note="T->A: Complete loss of aphid transmission and
FT binding to virions."
FT /evidence="ECO:0000269|PubMed:9568986"
FT MUTAGEN 619
FT /note="T->S,V: Strongly reduced aphid transmission and
FT binding to virions."
FT /evidence="ECO:0000269|PubMed:9568986"
FT MUTAGEN 620
FT /note="K->E: Slightly reduced aphid transmission and
FT binding to virions."
FT /evidence="ECO:0000269|PubMed:9568986"
FT CONFLICT 2694..2695
FT /note="LE -> ST (in Ref. 2; AAA48511)"
FT /evidence="ECO:0000305"
FT CONFLICT 2699..2701
FT /note="IVS -> LFP (in Ref. 2; AAA48511)"
FT /evidence="ECO:0000305"
FT CONFLICT 2811
FT /note="A -> T (in Ref. 2; AAA48511)"
FT /evidence="ECO:0000305"
FT CONFLICT 2834
FT /note="G -> S (in Ref. 2; AAA48511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3080 AA; 350629 MW; 2A1E501DEA6B9F73 CRC64;
MASIMIGSIS VPIAKTEQCA NTQVSNRANI VAPGHMATCP LPLKTHMYYR HESKKLMQSN
KSIDILNNFF STDEMKFRLT RNEMSKLKKG PSGRIVLRKP SKQRVFARIE QDEAARKEEA
VFLEGNYDDS ITNLARVLPP AVTHNVDVSL RSPFYKRTYK KERKKVAQKQ IVQAPLNSLC
TRVLKIARNK NIPVEMIGNK KTRHTLTFKR FRGCFVGKVS VAHEEGRMRH TEMSYEQFKW
LLKAICQVTH TERIREEDIK PGCSGWVLGT NHTLTKRYSR LPHLVIRGRD DDGIVNALEQ
VLFYSEVDHS SSQPEVQFFQ GWRRIFDKFR PSPDHVCKAD HNNEECGELA AIFCQALFPV
VKLSCQTCRE SLVEVSFEEF KDSLNANFII HKDEWGSFKE GSQYDNIFKL IKVATQATQN
LKLSSEVMKL VQNHTSTHMK QIQDINKALM KGSLVAQDEL DLALKQLLEM TQWFKNHMHL
TGEEALKMFR NKRSSKAMIN PSLLCGNQLD KNGNFVWGER GYHSKRLFKN FFEEVIPSEG
YTKYVVRNFP NGTRKLAIGS LIVPLNLDRA RTALLGESIE KKPLTSACVS QQNGNYIHSC
CCVTMDDGTP MYSELKSPTK RHLVIGASSD PKYIDLPASE AERMYIAKEG YCYLSIFLAM
LVNVNENEAK DFTKMIRDVL IPMLGQWPSL MDVATAAYIL GVFHPETRCA ELPRILVDHA
TQTMHVIDSY GSLTVGYHVL KAGTVNHLIQ FASNDLQSEM KHYRVGGTPT QRIKLEEQLI
KGIFKPKLMM QLLHDDPYIL LLGMISPTIL VHMYRMRHFE RGIEIWIKRD HEIGKIFVIL
EQLTRKVALA EVLVDQLNLI SEASPHLLEI MKGCQDNQRA YVPALDLLTI QVEREFSNKE
LKTNGYPDLQ QTLFDMREKM YAKQLHNSWQ ELSLLEKSCV TVRLKQFSIF TERNLIQRAK
EGKRASSLQF VHECFITTRV HAKSIRDAGV RKLNEALVGT CKFFFSCGFK IFARCYSDII
YLVNVCLVFS LVLQMSNTVR SMIAATREEK ERAMANKADE NERTLMHMYH IFSKKQDDAP
IYNDFLEHVR NVRPDLEETL LYMAGVEVVS TQAKSAVQIQ FEKIIAVLAL LTMCFDAERS
DAIFKILTKL KTVFGTVGET VRLQGLEDIE SLEDDKRLTI DFDINTNEAH SSTTFDVHFD
DWWNRQLQQN RTVPHYRTTG KFLEFTRNTA AFVANEIASS SEGEFLVRGR VGSGKSTSLP
AHLAKKGKVL LLEPTRPLAE NVSRQLAGDP FFQNVTLRMR GLSCFGSSNI TVMTSGFAFH
YYVNNPHQLM EFDFVIIDEC HVTDSATIAF NCALKEYNFA GKLIKVSATP PGRECDFDTQ
FAVKVKTEDH LSFHAFVGAQ KTGSNADMVQ HGNNILVYVA SYNEVDMLSK LLTERQFSVT
KVDGRTMQLG KTTIETHGTS QKPHFIVATN IIENGVTLDV ECVVDFGLKV GRRTGQRNRC
VRYNKKSVSY GERIQRLGRV GRSKPGTALR IGHTEKGIET IPEFIATEAA ALSFAYGLPV
TTHGVSTNIL GKCTVKQMKC ALNFELTPFF TTHLIRHDGS MHPLIHEELK QFKLRDSEMV
LNKVALPHQF VSQWMDQSEY ERIGVHVQCH ESNSIPFYTN GIPDKVYERI WKCIQENKND
AVFGKLSSAC STKVSYTLST DPAALPRTIA IIDHLLAEEM MKRNHFDTIS SAVTGYSFSL
AGIADSFRKR YMRDYTAHNI AILQQARAQL LEFNSKNVNI NNLSDLEGIG VIKSVVLQSK
QEVSSFLGLR GKWDGKKFAN DVILAIMTLL GGGWFMWEYF TKKINEPVRV ESKKRRSQKL
KFRDAYDRKV GREIFGDDDT IGRTFGEAYT KRGKVKGNNN TKGMGRKTRN FVHLYGVEPE
NYSFIRFVDP LTGHTLDEST HTDISLVQEE FGSIREKFLE NDLISRQSII NKPGIQAYFM
GKGTEEALKV DLTPHVPLLL CRNTNAIAGY PERENELRQT GTPVKVSFKD VPEKNEHVEL
ESKSIYKGVR DYNGISTIVC QLTNDSDGLK ETMYGIGYGP IIITNGHLFR KNNGTLLVRS
WHGEFIVKNT TTLKVHFIEG KDVVLVRMPK DFPPFKSNAS FRAPKREERR CLVGTNFQEK
SLRSTVSESS MTIPEGTGSY WIHWISTNEG DCGLPMVSTT DGKIIGVHGL ASTVSSKNYF
VPFTDDFIAT HLSKLDDLTW TQHWLWQPSK IAWGTLNLVD EQPGPEFRIS NLVKDLFTSG
VETQSKRERW VYESCEGNLR AVGTAQSALV TKHVVKGKCP FFEEYLQTHA EASAYFRPLM
GEYQPSKLNK EAFKKDFFKY NKPVTVNQLD HDKFLGAVDG VIRMMCDFEF NECRFITDPE
EIYNSLNMKA AIGAQYRGKK KEYFEGLDDF DRERLLFQSC ERLFNGYKGL WNGSLKAELR
PLEKVRANKT RTFTAAPIDT LLGAKVCVDD FNNEFYRKNL KCPWTVGMTK FYGGWDKLMR
SLPDGWLYCH ADGSQFDSSL TPALLNAVLI IRSFYMEDWW VGQEMLENLY AEIVYTPILA
PDGTIFKKFR GNNSGQPSTV VDNTLMVVIS IYYACMKFGW NCEEIENKLV FFANGDDLIL
AVKDEDSGLL DNMSSSFCEL GLNYDFSERT HKREDLWFMS HQAMLVDGMY TPKLEKERIV
SILEWDRSKE IMHRTEAICA AMIEAWGHTE LLQEIRKFYL WFVEKEEVRE LAALGKAPYI
AETALRKLYT DKGADTSELA RYLQALHQDI FFEQGDTVML QSGTQPTVAD AGATKKDKED
DKGKNKDVTG SGSGEKTVAA VTKDKDVNAG SHGKIVPRLS KITKKMSLPR VKGNVILDID
HLLEYKPDQI ELYNTRASHQ QFASWFNQVK TEYDLNEQQM GVVMNGFMVW CIENGTSPDI
NGVWVMMDGN EQVEYPLKPI VENAKPTLRQ IMHHFSDAAE AYIEMRNAEA PYMPRYGLLR
NLRDRSLARY AFDFYEVNSK TPERAREAVA QMKAAALSNV SSRLFGLDGN VATTSEDTER
HTARDVNRNM HTLLGVNTMQ
