MOD5_YEAST
ID MOD5_YEAST Reviewed; 428 AA.
AC P07884; D6W2X4; Q12203;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=tRNA dimethylallyltransferase;
DE Short=DMATase;
DE EC=2.5.1.75 {ECO:0000269|PubMed:18852462, ECO:0000269|PubMed:3031456};
DE AltName: Full=Isopentenyl-diphosphate: tRNA isopentenyltransferase;
DE Short=IPP transferase;
DE Short=IPPT;
DE AltName: Full=tRNA isopentenyltransferase;
DE Short=IPTase;
GN Name=MOD5; OrderedLocusNames=YOR274W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031457; DOI=10.1128/mcb.7.1.185-191.1987;
RA Najarian D., Dihanich M.E., Martin N.C., Hopper A.K.;
RT "DNA sequence and transcript mapping of MOD5: features of the 5' region
RT which suggest two translational starts.";
RL Mol. Cell. Biol. 7:185-191(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3031456; DOI=10.1128/mcb.7.1.177-184.1987;
RA Dihanich M.E., Najarian D., Clark R., Gillman E.C., Martin N.C.,
RA Hopper A.K.;
RT "Isolation and characterization of MOD5, a gene required for
RT isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 7:177-184(1987).
RN [6]
RP ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=1946403; DOI=10.1073/pnas.88.21.9789;
RA Slusher L.B., Gillman E.C., Martin N.C., Hopper A.K.;
RT "mRNA leader length and initiation codon context determine alternative AUG
RT selection for the yeast gene MOD5.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9789-9793(1991).
RN [7]
RP ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=1850093; DOI=10.1128/mcb.11.5.2382-2390.1991;
RA Gillman E.C., Slusher L.B., Martin N.C., Hopper A.K.;
RT "MOD5 translation initiation sites determine N6-isopentenyladenosine
RT modification of mitochondrial and cytoplasmic tRNA.";
RL Mol. Cell. Biol. 11:2382-2390(1991).
RN [8]
RP ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=8139535; DOI=10.1128/mcb.14.4.2298-2306.1994;
RA Boguta M., Hunter L.A., Shen W.C., Gillman E.C., Martin N.C., Hopper A.K.;
RT "Subcellular locations of MOD5 proteins: mapping of sequences sufficient
RT for targeting to mitochondria and demonstration that mitochondrial and
RT nuclear isoforms commingle in the cytosol.";
RL Mol. Cell. Biol. 14:2298-2306(1994).
RN [9]
RP FUNCTION.
RX PubMed=10618371; DOI=10.1073/pnas.97.1.61;
RA Benko A.L., Vaduva G., Martin N.C., Hopper A.K.;
RT "Competition between a sterol biosynthetic enzyme and tRNA modification in
RT addition to changes in the protein synthesis machinery causes altered
RT nonsense suppression.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:61-66(2000).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION.
RX PubMed=21873461; DOI=10.1261/rna.2628611;
RA Lamichhane T.N., Blewett N.H., Maraia R.J.;
RT "Plasticity and diversity of tRNA anticodon determinants of substrate
RT recognition by eukaryotic A37 isopentenyltransferases.";
RL RNA 17:1846-1857(2011).
RN [12]
RP PRION FORMATION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22517861; DOI=10.1126/science.1219491;
RA Suzuki G., Shimazu N., Tanaka M.;
RT "A yeast prion, Mod5, promotes acquired drug resistance and cell survival
RT under environmental stress.";
RL Science 336:355-359(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 13-421 IN COMPLEXES WITH
RP SUBSTRATE TRNA; ISOPENTENYL DIPHOSPHATE AND ZINC IONS, AND CATALYTIC
RP ACTIVITY.
RX PubMed=18852462; DOI=10.1073/pnas.0805680105;
RA Zhou C., Huang R.H.;
RT "Crystallographic snapshots of eukaryotic dimethylallyltransferase acting
RT on tRNA: insight into tRNA recognition and reaction mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16142-16147(2008).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 in the anticodon loop on a specific subset of
CC tRNAs both in the cytosol and the mitochondrion, leading to the
CC formation of N6-(dimethylallyl)adenosine (i(6)A). This modification
CC optimizes the codon:anticodon fit in the ribosome and promotes
CC translational fidelity. Competes with the farnesyl pyrophosphate
CC synthase ERG20 for the common substrate dimethylallyl diphosphate
CC (DMAPP). {ECO:0000269|PubMed:10618371, ECO:0000269|PubMed:21873461,
CC ECO:0000269|PubMed:3031456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC Evidence={ECO:0000269|PubMed:18852462, ECO:0000269|PubMed:3031456};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26483;
CC Evidence={ECO:0000269|PubMed:18852462, ECO:0000269|PubMed:3031456};
CC -!- SUBCELLULAR LOCATION: Note=[MOD+] forms multicytoplasmic aggregates
CC that do not colocalize to either mitochondria or nucleus.
CC {ECO:0000269|PubMed:22517861}.
CC -!- SUBCELLULAR LOCATION: [Isoform I]: Cytoplasm
CC {ECO:0000269|PubMed:1850093, ECO:0000269|PubMed:8139535}. Mitochondrion
CC {ECO:0000269|PubMed:1850093, ECO:0000269|PubMed:1946403,
CC ECO:0000269|PubMed:8139535}.
CC -!- SUBCELLULAR LOCATION: [Isoform II]: Cytoplasm
CC {ECO:0000269|PubMed:1850093, ECO:0000269|PubMed:1946403,
CC ECO:0000269|PubMed:8139535}. Nucleus {ECO:0000269|PubMed:8139535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=I; Synonyms=IPPT-I {ECO:0000303|PubMed:8139535};
CC IsoId=P07884-1; Sequence=Displayed;
CC Name=II; Synonyms=IPPT-II {ECO:0000303|PubMed:8139535};
CC IsoId=P07884-2; Sequence=VSP_018811;
CC -!- DOMAIN: The core aggregation region, although lacking the prion-typical
CC Gln/Asn (Q/N)-rich domain, is required for the formation of the
CC amyloid-like fibrillar aggregates. {ECO:0000305|PubMed:22517861}.
CC -!- MISCELLANEOUS: [MOD+] is the prion form of MOD5. [MOD+] is the result
CC of a conformational change of the cellular MOD5 protein that becomes
CC self-propagating and infectious. This conformational change generates a
CC form of MOD5 that assembles into amyloid-like fibrillar aggregates.
CC [MOD+]-aggregates sequester soluble MOD5, resulting in decreased levels
CC of (i(6)A)-modified tRNAs and higher ergosterol levels, due to less
CC competition for ERG20, which uses the same substrate DMAPP than MOD5.
CC [MOD+] can be cured by GdnHCl and by deletion of the molecular
CC chaperone HSP104, which is required for [MOD+] propagation. The [MOD+]
CC state acquires resistance against antifungal agents such as
CC flucanozole, ketoconazole and clotrimazole that inhibit ergosterol
CC biosynthesis. De novo appearance of [MOD+] is favored in the presence
CC of antifungal agents, and the growth advantage of [MOD+] is lost when
CC the cells are released from the selective pressure. Thus, the
CC conformational switch of MOD5 from a soluble state to a prion state
CC allows the cell to adapt to the harmful environment of anti-fungal
CC drugs by up-regulating ergosterol biosynthesis at the expense of tRNA
CC modification. {ECO:0000305|PubMed:22517861}.
CC -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; M15991; AAA34785.1; -; Genomic_DNA.
DR EMBL; X89633; CAA61780.1; -; Genomic_DNA.
DR EMBL; Z75182; CAA99499.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11040.1; -; Genomic_DNA.
DR PIR; S67176; S67176.
DR RefSeq; NP_014917.3; NM_001183693.3. [P07884-1]
DR PDB; 3EPH; X-ray; 2.95 A; A/B=13-421.
DR PDB; 3EPJ; X-ray; 3.10 A; A/B=13-421.
DR PDB; 3EPK; X-ray; 3.20 A; A/B=13-421.
DR PDB; 3EPL; X-ray; 3.60 A; A/B=13-421.
DR PDBsum; 3EPH; -.
DR PDBsum; 3EPJ; -.
DR PDBsum; 3EPK; -.
DR PDBsum; 3EPL; -.
DR AlphaFoldDB; P07884; -.
DR SMR; P07884; -.
DR BioGRID; 34663; 106.
DR DIP; DIP-4094N; -.
DR IntAct; P07884; 2.
DR STRING; 4932.YOR274W; -.
DR MaxQB; P07884; -.
DR PaxDb; P07884; -.
DR PRIDE; P07884; -.
DR EnsemblFungi; YOR274W_mRNA; YOR274W; YOR274W. [P07884-1]
DR GeneID; 854448; -.
DR KEGG; sce:YOR274W; -.
DR SGD; S000005800; MOD5.
DR VEuPathDB; FungiDB:YOR274W; -.
DR eggNOG; KOG1384; Eukaryota.
DR GeneTree; ENSGT00390000015214; -.
DR HOGENOM; CLU_032616_2_3_1; -.
DR InParanoid; P07884; -.
DR OMA; YAKRQYT; -.
DR BioCyc; YEAST:YOR274W-MON; -.
DR BRENDA; 2.5.1.75; 984.
DR EvolutionaryTrace; P07884; -.
DR PRO; PR:P07884; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07884; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IDA:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR030666; IPP_transferase_euk.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR PIRSF; PIRSF039110; IPP_transferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Amyloid; ATP-binding; Cytoplasm;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Prion;
KW Reference proteome; Transferase; tRNA processing; Zinc; Zinc-finger.
FT CHAIN 1..428
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000019025"
FT ZN_FING 373..409
FT /note="Matrin-type"
FT REGION 46..49
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT REGION 170..174
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT REGION 199..207
FT /note="Core aggregation region"
FT /evidence="ECO:0000269|PubMed:18852462"
FT REGION 210..232
FT /note="Interaction with isopentenylpyrophosphate
FT transferase"
FT /evidence="ECO:0000269|PubMed:18852462"
FT REGION 256..258
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT REGION 284..302
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 23..28
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:18852462"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18852462,
FT ECO:0007744|PDB:3EPH, ECO:0007744|PDB:3EPJ,
FT ECO:0007744|PDB:3EPK, ECO:0007744|PDB:3EPL"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18852462,
FT ECO:0007744|PDB:3EPH, ECO:0007744|PDB:3EPJ,
FT ECO:0007744|PDB:3EPK, ECO:0007744|PDB:3EPL"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18852462,
FT ECO:0007744|PDB:3EPH, ECO:0007744|PDB:3EPJ,
FT ECO:0007744|PDB:3EPK, ECO:0007744|PDB:3EPL"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18852462,
FT ECO:0007744|PDB:3EPH, ECO:0007744|PDB:3EPJ,
FT ECO:0007744|PDB:3EPK, ECO:0007744|PDB:3EPL"
FT SITE 112
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT SITE 193
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000269|PubMed:18852462"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_018811"
FT CONFLICT 313
FT /note="Missing (in Ref. 1; AAA34785)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="C -> R (in Ref. 1; AAA34785)"
FT /evidence="ECO:0000305"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 278..302
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3EPH"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:3EPH"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:3EPH"
FT HELIX 401..418
FT /evidence="ECO:0007829|PDB:3EPH"
SQ SEQUENCE 428 AA; 50237 MW; A956B17ABC05161F CRC64;
MLKGPLKGCL NMSKKVIVIA GTTGVGKSQL SIQLAQKFNG EVINSDSMQV YKDIPIITNK
HPLQEREGIP HHVMNHVDWS EEYYSHRFET ECMNAIEDIH RRGKIPIVVG GTHYYLQTLF
NKRVDTKSSE RKLTRKQLDI LESTDPDVIY NTLVKCDPDI ATKYHPNDYR RVQRMLEIYY
KTGKKPSETF NEQKITLKFD TLFLWLYSKP EPLFQRLDDR VDDMLERGAL QEIKQLYEYY
SQNKFTPEQC ENGVWQVIGF KEFLPWLTGK TDDNTVKLED CIERMKTRTR QYAKRQVKWI
KKMLIPDIKG DIYLLDATDL SQWDTNASQR AIAISNDFIS NRPIKQERAP KALEELLSKG
ETTMKKLDDW THYTCNVCRN ADGKNVVAIG EKYWKIHLGS RRHKSNLKRN TRQADFEKWK
INKKETVE
