AFG2_YEAST
ID AFG2_YEAST Reviewed; 780 AA.
AC P32794; D6VZ32;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=ATPase family gene 2 protein {ECO:0000303|PubMed:8109176};
DE EC=3.6.4.10 {ECO:0000269|PubMed:12006565, ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:24371142};
DE AltName: Full=Diazaborine resistance gene 1 protein {ECO:0000303|PubMed:12006565};
GN Name=AFG2 {ECO:0000303|PubMed:8109176, ECO:0000312|SGD:S000004389};
GN Synonyms=DRG1 {ECO:0000303|PubMed:12006565}; OrderedLocusNames=YLR397C;
GN ORFNames=L8084.16;
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], AND FUNCTION.
RX PubMed=8109176; DOI=10.1002/yea.320091114;
RA Thorsness P.E., White K.H., Ong W.-C.;
RT "AFG2, an essential gene in yeast, encodes a new member of the Sec18p,
RT Pas1p, Cdc48p, TBP-1 family of putative ATPases.";
RL Yeast 9:1267-1271(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF PHE-343; LEU-457; CYS-561; SER-562 AND VAL-725.
RX PubMed=12006565; DOI=10.1074/jbc.m201515200;
RA Zakalskiy A., Hoegenauer G., Ishikawa T., Wehrschuetz-Sigl E., Wendler F.,
RA Teis D., Zisser G., Steven A.C., Bergler H.;
RT "Structural and enzymatic properties of the AAA protein Drg1p from
RT Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase
RT activity and hexamerization.";
RL J. Biol. Chem. 277:26788-26795(2002).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE PRE-60S COMPLEX, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF PHE-343; LEU-457 AND GLU-617.
RX PubMed=17646390; DOI=10.1128/mcb.00668-07;
RA Pertschy B., Saveanu C., Zisser G., Lebreton A., Tengg M., Jacquier A.,
RA Liebminger E., Nobis B., Kappel L., van der Klei I., Hoegenauer G.,
RA Fromont-Racine M., Bergler H.;
RT "Cytoplasmic recycling of 60S preribosomal factors depends on the AAA
RT protein Drg1.";
RL Mol. Cell. Biol. 27:6581-6592(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, INTERACTION WITH RLP24, DOMAIN, AND MUTAGENESIS OF
RP GLU-346; LEU-457 AND GLU-617.
RX PubMed=23185031; DOI=10.1083/jcb.201205021;
RA Kappel L., Loibl M., Zisser G., Klein I., Fruhmann G., Gruber C.,
RA Unterweger S., Rechberger G., Pertschy B., Bergler H.;
RT "Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S
RT maturation.";
RL J. Cell Biol. 199:771-782(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RLP24,
RP DOMAIN, AND MUTAGENESIS OF GLU-346; CYS-561; ALA-569; GLU-617 AND VAL-725.
RX PubMed=24371142; DOI=10.1074/jbc.m113.536110;
RA Loibl M., Klein I., Prattes M., Schmidt C., Kappel L., Zisser G., Gungl A.,
RA Krieger E., Pertschy B., Bergler H.;
RT "The drug diazaborine blocks ribosome biogenesis by inhibiting the AAA-
RT ATPase Drg1.";
RL J. Biol. Chem. 289:3913-3922(2014).
CC -!- FUNCTION: ATP-dependent chaperone which uses the energy provided by ATP
CC hydrolysis to generate mechanical force to disassemble protein
CC complexes (PubMed:12006565, PubMed:17646390, PubMed:23185031,
CC PubMed:24371142). Plays an essential role in the cytoplasmic maturation
CC steps of pre-60S ribosomal particles by promoting the release of
CC shuttling protein RLP24 from the pre-ribosomal particles
CC (PubMed:17646390, PubMed:23185031, PubMed:24371142). This step
CC facilitates the subsequent release of other shuttling proteins such as
CC NOG1 and allows the transition of the pre-ribosomal particles to later
CC maturation forms that bind REI1 (PubMed:17646390, PubMed:23185031,
CC PubMed:24371142). Essential for viability (PubMed:8109176,
CC PubMed:24371142). {ECO:0000269|PubMed:12006565,
CC ECO:0000269|PubMed:17646390, ECO:0000269|PubMed:23185031,
CC ECO:0000269|PubMed:24371142, ECO:0000269|PubMed:8109176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000269|PubMed:12006565, ECO:0000269|PubMed:23185031,
CC ECO:0000269|PubMed:24371142};
CC -!- ACTIVITY REGULATION: The hexamer is activated by RLP24 during pre-60S
CC ribosomal particle maturation; RLP24 activates ATPase activity of both
CC ATP-binding regions and increases cooperativity between AFG2 subunits
CC (PubMed:23185031). The second ATP-binding region is inhibited by
CC diazaborine; the inhibition requires prior ATP binding specifically to
CC the second ATP-binding region (PubMed:24371142).
CC {ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:24371142}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for ATP {ECO:0000269|PubMed:12006565};
CC KM=270 uM for ATP {ECO:0000269|PubMed:23185031};
CC Vmax=1.99 umol/h/mg enzyme {ECO:0000269|PubMed:23185031};
CC Vmax=28.7 umol/h/mg enzyme (in presence of RLP24)
CC {ECO:0000269|PubMed:23185031};
CC -!- SUBUNIT: Homohexamer; ATP binding induces oligomerization
CC (PubMed:12006565, PubMed:23185031). Forms a ring-shaped particle of
CC about 12 nm diameter, that displays 6-fold radial symmetry
CC (PubMed:12006565). Associates with cytoplasmic pre-60S ribosomal
CC particles containing ARX1, ALB1, RLP24 and NOG1 (PubMed:17646390).
CC Binds to pre-60S ribosomal particles soon after their export from the
CC nucleus and is released before REI1 and LSG1 are incorporated into the
CC particles (PubMed:17646390). Hexameric form interacts with RLP24 (via
CC C-terminal); the interaction recruits AFG2 to pre-60S ribosomal
CC particles and promotes AFG2 ATPase activity and RLP24 release from pre-
CC 60S ribosomal particles (PubMed:23185031, PubMed:24371142). Interacts
CC (via N-terminus) with nucleoporin NUP116 (via N-terminus); the
CC interaction is required for RLP24 release from pre-60S ribosomal
CC particles (PubMed:23185031). {ECO:0000269|PubMed:12006565,
CC ECO:0000269|PubMed:17646390, ECO:0000269|PubMed:23185031,
CC ECO:0000269|PubMed:24371142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17646390}.
CC -!- DOMAIN: The first ATP-binding region binds ATP with low affinity
CC whereas the second ATP-binding region binds ATP with high affinity
CC (PubMed:12006565). ATP hydrolysis mediated by the second ATP binding
CC region releases RLP24 from pre-60S ribosomal particles whereas the ATP
CC hydrolysis mediated by the first ATP binding region is subsequently
CC required for RLP24 dissociation from AFG2, probably by disassembling
CC AFG2 into monomers (PubMed:23185031, PubMed:24371142).
CC {ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:24371142,
CC ECO:0000305|PubMed:12006565}.
CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {ECO:0000305}.
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DR EMBL; L14615; AAC37367.1; -; Unassigned_DNA.
DR EMBL; U19729; AAB82355.1; -; Genomic_DNA.
DR EMBL; AY693116; AAT93135.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09698.1; -; Genomic_DNA.
DR PIR; S39110; S39110.
DR RefSeq; NP_013501.1; NM_001182285.1.
DR PDB; 7NKU; EM; 3.40 A; A/B/C/D/E/F=1-780.
DR PDBsum; 7NKU; -.
DR AlphaFoldDB; P32794; -.
DR SMR; P32794; -.
DR BioGRID; 31656; 327.
DR DIP; DIP-4470N; -.
DR IntAct; P32794; 10.
DR MINT; P32794; -.
DR STRING; 4932.YLR397C; -.
DR MaxQB; P32794; -.
DR PaxDb; P32794; -.
DR PRIDE; P32794; -.
DR EnsemblFungi; YLR397C_mRNA; YLR397C; YLR397C.
DR GeneID; 851113; -.
DR KEGG; sce:YLR397C; -.
DR SGD; S000004389; AFG2.
DR VEuPathDB; FungiDB:YLR397C; -.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00940000157323; -.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; P32794; -.
DR OMA; RAPDLCD; -.
DR BioCyc; YEAST:G3O-32461-MON; -.
DR PRO; PR:P32794; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32794; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0034214; P:protein hexamerization; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Reference proteome; Repeat; Ribosome biogenesis.
FT CHAIN 1..780
FT /note="ATPase family gene 2 protein"
FT /id="PRO_0000084592"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:12006565"
FT BINDING 557..564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:12006565"
FT MUTAGEN 343
FT /note="F->L: In dgr1-sup*; moderate loss of catalytic
FT activity. No growth defect. Restores growth and formation
FT of 60S ribosomal subunit maturation but not catalytic
FT activity or oligomerization; when associated with S-457."
FT /evidence="ECO:0000269|PubMed:12006565"
FT MUTAGEN 346
FT /note="E->Q: Reduces basal and RLP24-dependent ATPase
FT activity. Increases interaction with RLP24. Slightly
FT reduces RLP24 release. Does not affect composition of pre-
FT 60S ribosomal particles or growth."
FT /evidence="ECO:0000269|PubMed:23185031,
FT ECO:0000269|PubMed:24371142"
FT MUTAGEN 457
FT /note="L->S: In afg2-18, drg1-18 or drg1-ts; temperature
FT sensitive mutant. At the restrictive temperature of 37
FT degree Celsius, impaired growth. Severe loss of ATPase
FT activity, homohexamer formation and 60S ribosomal subunit
FT maturation. Prevents the release of shuttling proteins
FT NOG1, RLP24 and ARX1 from cytoplasmic pre-60S particles
FT resulting in their cytoplasmic accumulation. Loss of
FT interaction with RLP24 and pre-60S particles. Restores
FT growth and formation of 60S ribosomal subunit maturation
FT but not catalytic activity or oligomerization; when
FT associated with L-343."
FT /evidence="ECO:0000269|PubMed:12006565,
FT ECO:0000269|PubMed:17646390, ECO:0000269|PubMed:23185031"
FT MUTAGEN 561..562
FT /note="CS->TG: Increases ATPase activity and reduces
FT affinity for ATP. Mild defect in oligomerization."
FT /evidence="ECO:0000269|PubMed:12006565"
FT MUTAGEN 561
FT /note="C->T: In drg1-11; severe loss of ATPase activity.
FT Severe loss of oligomerization. Resistant to diazaborine-
FT mediated growth inhibition."
FT /evidence="ECO:0000269|PubMed:12006565"
FT MUTAGEN 562
FT /note="S->G: Increases ATPase activity. Loss of
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:12006565"
FT MUTAGEN 569
FT /note="A->V: In drg1-3; resistant to diazaborine-mediated
FT growth inhibition."
FT /evidence="ECO:0000269|PubMed:24371142"
FT MUTAGEN 617
FT /note="E->Q: Increases basal ATPase activity. Reduces
FT RLP24-mediated activation. Does not affect interaction with
FT RLP24. Prevents the release of shuttling proteins RLP24,
FT NOG1 and MEX67 from cytoplasmic pre-60S ribosomal
FT particles. Does not affect the interaction with pre-60S
FT ribosomal particles."
FT /evidence="ECO:0000269|PubMed:17646390,
FT ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:24371142"
FT MUTAGEN 725
FT /note="V->E: In drg1-1; slight loss of ATPase activity. No
FT effect on affinity for ATP or oligomerization. Resistant to
FT diazaborine-mediated growth inhibition. No defect in RLP24
FT release from pre-60S ribosomal particles in the absence or
FT in the presence of diazaborine."
FT /evidence="ECO:0000269|PubMed:12006565,
FT ECO:0000269|PubMed:24371142"
FT MUTAGEN 725
FT /note="V->L: In drg1-4; resistant to diazaborine-mediated
FT growth inhibition."
FT /evidence="ECO:0000269|PubMed:24371142"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 455..475
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 488..498
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 522..536
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 576..583
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 584..587
FT /evidence="ECO:0007829|PDB:7NKU"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 593..607
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 628..644
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 651..660
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 674..680
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:7NKU"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 709..715
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 721..738
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 747..756
FT /evidence="ECO:0007829|PDB:7NKU"
FT HELIX 763..775
FT /evidence="ECO:0007829|PDB:7NKU"
SQ SEQUENCE 780 AA; 84748 MW; 75094DFA3D401D4E CRC64;
MAPKSSSSGS KKKSSASSNS ADAKASKFKL PAEFITRPHP SKDHGKETCT AYIHPNVLSS
LEINPGSFCT VGKIGENGIL VIARAGDEEV HPVNVITLST TIRSVGNLIL GDRLELKKAQ
VQPPYATKVT VGSLQGYNIL ECMEEKVIQK LLDDSGVIMP GMIFQNLKTK AGDESIDVVI
TDASDDSLPD VSQLDLNMDD MYGGLDNLFY LSPPFIFRKG STHITFSKET QANRKYNLPE
PLSYAAVGGL DKEIESLKSA IEIPLHQPTL FSSFGVSPPR GILLHGPPGT GKTMLLRVVA
NTSNAHVLTI NGPSIVSKYL GETEAALRDI FNEARKYQPS IIFIDEIDSI APNRANDDSG
EVESRVVATL LTLMDGMGAA GKVVVIAATN RPNSVDPALR RPGRFDQEVE IGIPDVDARF
DILTKQFSRM SSDRHVLDSE AIKYIASKTH GYVGADLTAL CRESVMKTIQ RGLGTDANID
KFSLKVTLKD VESAMVDIRP SAMREIFLEM PKVYWSDIGG QEELKTKMKE MIQLPLEASE
TFARLGISAP KGVLLYGPPG CSKTLTAKAL ATESGINFLA VKGPEIFNKY VGESERAIRE
IFRKARSAAP SIIFFDEIDA LSPDRDGSST SAANHVLTSL LNEIDGVEEL KGVVIVAATN
RPDEIDAALL RPGRLDRHIY VGPPDVNARL EILKKCTKKF NTEESGVDLH ELADRTEGYS
GAEVVLLCQE AGLAAIMEDL DVAKVELRHF EKAFKGIARG ITPEMLSYYE EFALRSGSSS
