POLG_BSTV1
ID POLG_BSTV1 Reviewed; 3093 AA.
AC Q65730;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE AltName: Full=N-terminal protein;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
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 Brome streak virus (strain 11-Cal) (BStV) (Brome streak mosaic rymovirus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Tritimovirus.
OX NCBI_TaxID=117138;
OH NCBI_TaxID=4501; Bromus.
OH NCBI_TaxID=97361; Hordeum murinum (Mouse barley) (Critesion murinum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7636484; DOI=10.1099/0022-1317-76-8-2035;
RA Goetz R., Maiss E.;
RT "The complete nucleotide sequence and genome organization of the mite-
RT transmitted brome streak mosaic rymovirus in comparison with those of
RT potyviruses.";
RL J. Gen. Virol. 76:2035-2042(1995).
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 -!- 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: [Capsid protein]: Virion {ECO:0000305}.
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]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; Z48506; CAA88417.1; -; Genomic_RNA.
DR RefSeq; NP_612585.1; NC_003501.1.
DR MINT; Q65730; -.
DR GeneID; 935897; -.
DR KEGG; vg:935897; -.
DR Proteomes; UP000000521; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
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: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; 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; IPR025910; P1_Ser_Pept_dom.
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; 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; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF13611; Peptidase_S76; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 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; 1.
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; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Reference proteome; RNA-directed RNA polymerase; Serine protease;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..3093
FT /note="Genome polyprotein"
FT /id="PRO_0000419992"
FT CHAIN 1..403
FT /note="P1 proteinase"
FT /id="PRO_0000040233"
FT CHAIN 404..809
FT /note="Helper component proteinase"
FT /id="PRO_0000040234"
FT CHAIN 810..1087
FT /note="Protein P3"
FT /id="PRO_0000040235"
FT CHAIN 1088..1138
FT /note="6 kDa protein 1"
FT /id="PRO_0000040236"
FT CHAIN 1139..1783
FT /note="Cytoplasmic inclusion protein"
FT /id="PRO_0000040237"
FT CHAIN 1784..1834
FT /note="6 kDa protein 2"
FT /id="PRO_0000040238"
FT CHAIN 1835..2040
FT /note="Viral genome-linked protein"
FT /id="PRO_0000040239"
FT CHAIN 2041..2275
FT /note="Nuclear inclusion protein A"
FT /id="PRO_0000040240"
FT CHAIN 2276..2773
FT /note="Nuclear inclusion protein B"
FT /id="PRO_0000040241"
FT CHAIN 2774..3093
FT /note="Capsid protein"
FT /id="PRO_0000040242"
FT DOMAIN 255..403
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 690..809
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1215..1366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1367..1546
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2041..2257
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2516..2639
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2800..2842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1316..1319
FT /note="DEVH box"
FT MOTIF 1883..1895
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2802..2834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 323
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 355
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 698
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 769
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2082
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2121
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2193
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1228..1235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 403..404
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 809..810
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1087..1088
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1138..1139
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1783..1784
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1834..1835
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2040..2041
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2275..2276
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2773..2774
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"
SQ SEQUENCE 3093 AA; 348106 MW; 50F775CEF7ABCCB4 CRC64;
MQQTHVKQVW RPKTASSKVK TSNMVYLAEE SSPLAKTELK EDAVVAADMS VINADDAVYG
HALEGKYSER KALPARSNET IVSFASGEDG LFLDRAACGS IFKTRTGKDT PIATAIRAAT
RRGLAYDIAA QLYMCPKCCS ASDKVLYFDT NHNDSCQWYL DNCRAVINKD WTLDVIETYN
VFPVLVTEEE ERRTLEAVDI ALKPLGTVPV HDVVQVYDQK IGEHKEVERN QEAAHGSEPA
IITTTPVLRR QCIEKRLLRH VHQANKVIAN TVEIYDLMTE TSQICAEKAI PLVFVDYEKK
KRIRPRVPLR HVLESNNVDP SDDLYADVVP FLKHYGTCGR PVGVINPRDI KPGWSGVVLL
QDELPESLHQ ECVDGVFVVQ GIGPDGQLKN ALKTTTGERI EYYSSKRRMA VNAHVPKAHS
FCKYSSLTET LMELDYLRVI SALADVHDPQ CVECHKERNE RSFIENLKYT QQGAQNLFNA
GTGMGLAFVA SIASGQLMIQ RQQPQSSSSI VDQTPRTNED GSLSHNINLL LTPEVVDIWR
SMKQMVHLPN RKLYMASFND QFGNFDFIPN STLQGVFPDF TMPVTIALND DDKVETNYRH
VDKNSTIETC VEGLYTQFDA AYWTKKAAQV HKIQPIDQCG MEIGNIALKL CHWEGDVALF
SPIIRPTPGH LMFGSTDRLL RIPDMTNARH YVPKVGYCYL YLFALAMNFC DGENRVTVDA
YINKTCRELG AWPKFGEVLR ALDRMATYYG CYDAVVPVML VDHVQRTIHV PSPFGIVQSG
MHMIQINNLG DLIKLDTMGA SELKEYEIGG FRETYKSITK CVKSKSAFME KLNQDNEWLV
DMICNPSTLF VLSQLMDTHG LILKDVENSF DRLAALLALK ELGSALGPLL TTRKRVALYM
QSLSKVDELV PHLGMPTGAM NLLKSEIELI QNAIVEEQDM AEIDRVEGKK SILERRDEMF
APCVYNEFIN SFGYVSLPGI AYRLTYTGVG ARIGRGCEHL KTVWSGSWIP EIHLPENLRS
NTWSAIKKYT VYSGGTAWRY MKLKIVESAT QILVAAVITA IGSWLLKKLL KFIRHEKGRL
NEVVVFQSKQ EELFISKFMA VCFVISTFFS LDMSNAIYSS LTKFRAIFSI LSVGSIYQSG
ALEKLEEQLG HVDTFHEFKL YDHDATHANI APSVQSFGTW LDTRVLAGQQ GCDPLEGRHT
KFEMNKNTRD AIAARVLADK DNEFLVMGHV GCGKSTYFPV ALSKQARVLI CEPTRVLVTN
LHDSMMHTCQ VAPSVMMRNH RCITGSSIMV QTYGFALHYL VNNPENLQQY DFVLFDEVHH
TCAEKVVLYN WLKGRDWGGK IVKLTATDRS PSAEIKAQKS LDIMTLPTMT PLDFVKEQGL
STKADASKHG KVILVFLTSF REVDSCYDEL KRKENFDAIK ADSRNLRNKT SLADLISECK
KEFIYIFATN ILQTGINIEA DVVVDFGYKI VPTYDVDNRM LTTTRKPVNK ADRIQRLGRV
ARMKAGVAMK IGATIDPEAY DDEVTATEAA LLSFAMQVPP VLRNVNLQIF QRITREQVVT
AARFEHQLSY MVWMVNKDGS MPTKLYDLFS PLLLSQGNMR LSPYYSSLYD SDTFMTVKNY
VDIGYLKHDR TTNQRLPFHC HDVSTTFAMK VADRFEDSRA PSTYSIRVPA VNLRHTAVKL
STDPAQVGMI LVVIGEALVH QKNILEQLKS TRTQLDNYNS CILVPNWNVR GKLDDAINRV
ERNVSILENQ KNSVEKMSVA RGYDELKELL EENHAVAAHV MYQKGPQKFI DDVLLQKRDF
SWMPYISVGA ACLMAGCAWY MLYRQRAKHE AKFEGKASRV KASKQKAFDD KMARADNYTY
YETTDELHNH AREWNDYPTD WVDKVRKKAN VHAMQFGREA PRRDVRNDRP FFNFYGIDEK
LYDTVTFHDM AASFSVEQPI TAMEVEEAFE KIYLNRQEDE AFFDHPMPKK ILAEFKGKDG
KVINVEMEPH NPRKANRRGL PVGYADHRGE FRQAKPAEEG PIKFERKALN PKATPYAVFE
SKALYGGPRC YEHITNNQVL LAGPSGYLNG LITGSKLLAP YHFVKDISSD SQDPSRMIAR
FGTYNLGNIL NLQVVKFTMI DLIGLDLPVE FQPRRTLKCF RVPVIGEKAV LVLSRYSKEG
WKSCVSAETE ITPYGENEEL LWRHRITTEV GDCGATMVAL SDQKIVGFHS LGGISMNYFV
PVTQELLDFL SSKTEKPLVP WRFSEDQVDV GGLYIHNDFD KFPFVKTIQK LVGFQNGHMI
KYCGEGFTPV ARSENRLSRQ HVISGQRESF IHFVEASSKW RPLITPMLGR LQPSALNREA
YYKDVLKYDK PIRLGTVHEE AFQSAVINVI RILENAGFER GGVKACFDYG KIFNDLNLDA
AMGALYAGKK KDYFVEATDE EIEEMFLRSA GKICANGHGV WSALLKAELR PAEKVAANKT
RTFTSAPIDI LFGAKAVVDD FNKQFYKRHL LGPWTVGINK FNKGWDLLAR SLMRYEWFID
ADGSQFDSSI TPLLMNAVLT IRLYFMERDD ITELMLRNLY TQIISTCMLA EDGLIVQKHR
GNNSGQPSTV VDNTLCLMIA MEYARQRAIS DGHLNMQMRY VCNGDDLLIN ANEEAKDVVQ
GKYEQYIKEL ELNYCFDDAF QSIEGVEFMS HKFMLRNGIY IPKLARHRIV AILEWQRSAE
PQAIKSAILA ACVEAFGYDD LTELIREYAI SLEPVWGSFL PTDGEIEQLY FEGIAKQEVA
RCLAGVDDVC KFESAASGTN EAVDEVLKAA GDDEALARAN AAATSGATTP AQNVGAGTTT
PAKATPQSGR RPSFGSLIDN PIGGNGVQDV ADRTSGIVFP VPTRKSTSLY LPPKVKLRAT
PERIEKVRKY LPDPQQIDLR YSTQQELNDW IKASADGLGQ TEEAFIDNIL PGWIVHCIVN
TTSSENRKAG SWRCVTNAGT ADEEQVLYDI EPMYSAANPT MRAIMRHFSD LARLVIAESF
KQGRPLIPKG YIKAGVLDAS SAAAACDFVV RDRHDTATFV QVQNQVLVNR VSGITNRLFA
QAMPSAGANE DMARHDAQDA AEGIHNLGGA RAF
