ID KU70_YEAST Reviewed; 602 AA. AC P32807; D6W0B1; P32498; Q0P778; Q0P779; Q0P787; Q0P789; Q6B267; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=ATP-dependent DNA helicase II subunit 1; DE EC=3.6.4.12; DE AltName: Full=ATP-dependent DNA helicase II subunit Ku70; DE AltName: Full=High affinity DNA-binding factor subunit 1; GN Name=YKU70; Synonyms=HDF1, NES24; OrderedLocusNames=YMR284W; GN ORFNames=YM8021.10; 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], PROTEIN SEQUENCE OF 4-20, AND SUBUNIT. RC STRAIN=ABYS 60; RX PubMed=8509423; DOI=10.1016/s0021-9258(18)31470-4; RA Feldmann H., Winnacker E.L.; RT "A putative homologue of the human autoantigen Ku from Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 268:12895-12900(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8017106; DOI=10.1002/yea.320100309; RA Yoshida M., Shimma Y., Uno I., Toh-e A.; RT "Cloning and sequencing of the NES24 gene of Saccharomyces cerevisiae."; RL Yeast 10:371-376(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, RC DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, and Y55; RX PubMed=16951060; DOI=10.1534/genetics.106.062166; RA Liti G., Barton D.B., Louis E.J.; RT "Sequence diversity, reproductive isolation and species concepts in RT Saccharomyces."; RL Genetics 174:839-850(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [5] 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 [6] 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 [7] RP FUNCTION IN TELOMERE MAINTENANCE AND MATING-TYPE SWITCHING. RX PubMed=8626469; DOI=10.1074/jbc.271.14.7910; RA Mages G.J., Feldmann H.M., Winnacker E.-L.; RT "Involvement of the Saccharomyces cerevisiae HDF1 gene in DNA double-strand RT break repair and recombination."; RL J. Biol. Chem. 271:7910-7915(1996). RN [8] RP FUNCTION. RX PubMed=8668537; DOI=10.1093/nar/24.11.2067; RA Tsukamoto Y., Kato J., Ideka H.; RT "Hdf1, a yeast Ku-protein homologue, is involved in illegitimate RT recombination, but not in homologous recombination."; RL Nucleic Acids Res. 24:2067-2072(1996). RN [9] RP FUNCTION IN TELOMERIC GENE SILENCING. RX PubMed=9914366; DOI=10.1007/s004120050318; RA Evans S.K., Sistrunk M.L., Nugent C.I., Lundblad V.; RT "Telomerase, Ku, and telomeric silencing in Saccharomyces cerevisiae."; RL Chromosoma 107:352-358(1998). RN [10] RP FUNCTION IN TELOMERE MAINTENANCE, AND SUBCELLULAR LOCATION. RX PubMed=9635192; DOI=10.1016/s0960-9822(98)70252-0; RA Laroche T., Martin S.G., Gotta M., Gorham H.C., Pryde F.E., Louis E.J., RA Gasser S.M.; RT "Mutation of yeast Ku genes disrupts the subnuclear organization of RT telomeres."; RL Curr. Biol. 8:653-656(1998). RN [11] RP FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE. RX PubMed=9635193; DOI=10.1016/s0960-9822(98)70253-2; RA Nugent C.I., Bosco G., Ross L.O., Evans S.K., Salinger A.P., Moore J.K., RA Haber J.E., Lundblad V.; RT "Telomere maintenance is dependent on activities required for end repair of RT double-strand breaks."; RL Curr. Biol. 8:657-660(1998). RN [12] RP FUNCTION IN TELOMERE MAINTENANCE. RX PubMed=9663392; DOI=10.1016/s0960-9822(98)70325-2; RA Polotnianka R.M., Li J., Lustig A.J.; RT "The yeast Ku heterodimer is essential for protection of the telomere RT against nucleolytic and recombinational activities."; RL Curr. Biol. 8:831-834(1998). RN [13] RP FUNCTION IN NON-HOMOLOGOUS END JOINING DNA REPAIR. RX PubMed=10675560; DOI=10.1016/s0014-5793(00)01180-7; RA de la Torre-Ruiz M., Lowndes N.F.; RT "The Saccharomyces cerevisiae DNA damage checkpoint is required for RT efficient repair of double strand breaks by non-homologous end joining."; RL FEBS Lett. 467:311-315(2000). RN [14] RP FUNCTION IN TELOMERASE AND CDC13 TELOMERE RECRUITMENT. RX PubMed=11046137; DOI=10.1128/mcb.20.22.8397-8408.2000; RA Grandin N., Damon C., Charbonneau M.; RT "Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate RT telomerase recruitment."; RL Mol. Cell. Biol. 20:8397-8408(2000). RN [15] RP FUNCTION IN TELOMERE RECOMBINATION. RX PubMed=12138180; DOI=10.1128/mcb.22.16.5679-5687.2002; RA Tsai Y.-L., Tseng S.-F., Chang S.-H., Lin C.-C., Teng S.-C.; RT "Involvement of replicative polymerases, Tel1p, Mec1p, Cdc13p, and the Ku RT complex in telomere-telomere recombination."; RL Mol. Cell. Biol. 22:5679-5687(2002). RN [16] RP FUNCTION IN TELOMERIC REPAIR AND BINDING TO TLC1 STEM LOOP. RX PubMed=12975323; DOI=10.1101/gad.1125903; RA Stellwagen A.E., Haimberger Z.W., Veatch J.R., Gottschling D.E.; RT "Ku interacts with telomerase RNA to promote telomere addition at native RT and broken chromosome ends."; RL Genes Dev. 17:2384-2395(2003). RN [17] RP FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE. RX PubMed=14585978; DOI=10.1128/mcb.23.22.8202-8215.2003; RA Bertuch A.A., Lundblad V.; RT "The Ku heterodimer performs separable activities at double-strand breaks RT and chromosome termini."; RL Mol. Cell. Biol. 23:8202-8215(2003). RN [18] 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 [19] RP SUMOYLATION BY MMS21. RX PubMed=15738391; DOI=10.1073/pnas.0500537102; RA Zhao X., Blobel G.; RT "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA RT repair and chromosomal organization."; RL Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-372, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. CC Involved in non-homologous end joining (NHEJ) DNA double strand break CC repair. DNA-binding is sequence-independent but has a high affinity to CC nicks in double-stranded DNA and to the ends of duplex DNA. Binds to CC naturally occurring chromosomal ends, and therefore provides CC chromosomal end protection. Appears to have a role in recruitment of CC telomerase and CDC13 to the telomere and the subsequent telomere CC elongation. Required also for telomere recombination to repair CC telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 CC heterodimer, binds to the stem loop of TLC1, the RNA component of CC telomerase. Involved in telomere maintenance. Interacts with telomeric CC repeats and subtelomeric sequences thereby controlling telomere length CC and protecting against subtelomeric rearrangement. Maintains telomeric CC chromatin, which is involved in silencing the expression of genes CC located at the telomere. Required for mating-type switching. CC {ECO:0000269|PubMed:10675560, ECO:0000269|PubMed:11046137, CC ECO:0000269|PubMed:12138180, ECO:0000269|PubMed:12975323, CC ECO:0000269|PubMed:14585978, ECO:0000269|PubMed:8626469, CC ECO:0000269|PubMed:8668537, ECO:0000269|PubMed:9635192, CC ECO:0000269|PubMed:9635193, ECO:0000269|PubMed:9663392, CC ECO:0000269|PubMed:9914366}. 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=3.6.4.12; CC -!- SUBUNIT: Heterodimer of YKU70/HDF1 and YKU80/HDF2. CC {ECO:0000269|PubMed:8509423}. CC -!- INTERACTION: CC P32807; Q12306: SMT3; NbExp=2; IntAct=EBI-8214, EBI-17490; CC P32807; Q04437: YKU80; NbExp=2; IntAct=EBI-8214, EBI-8224; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9635192}. Chromosome, CC telomere {ECO:0000269|PubMed:9635192}. CC -!- PTM: Sumoylated by MMS21. {ECO:0000269|PubMed:15738391}. CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X70379; CAA49840.1; -; Genomic_DNA. DR EMBL; D15052; BAA03648.1; -; Genomic_DNA. DR EMBL; AM296304; CAL36013.1; -; Genomic_DNA. DR EMBL; AM296302; CAL36015.1; -; Genomic_DNA. DR EMBL; AM296301; CAL36016.1; -; Genomic_DNA. DR EMBL; AM296299; CAL36018.1; -; Genomic_DNA. DR EMBL; AM296298; CAL36019.1; -; Genomic_DNA. DR EMBL; AM296297; CAL36020.1; -; Genomic_DNA. DR EMBL; AM296296; CAL36021.1; -; Genomic_DNA. DR EMBL; AM296294; CAL36023.1; -; Genomic_DNA. DR EMBL; AM296292; CAL36025.1; -; Genomic_DNA. DR EMBL; AM296295; CAL36022.1; -; Genomic_DNA. DR EMBL; AM296303; CAL36014.1; -; Genomic_DNA. DR EMBL; AM296293; CAL36024.1; -; Genomic_DNA. DR EMBL; Z49704; CAA89782.1; -; Genomic_DNA. DR EMBL; AY692863; AAT92882.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10185.1; -; Genomic_DNA. DR PIR; S54591; S54591. DR RefSeq; NP_014011.1; NM_001182791.1. DR PDB; 5Y58; X-ray; 2.80 A; A/C/E=28-602. DR PDBsum; 5Y58; -. DR AlphaFoldDB; P32807; -. DR SMR; P32807; -. DR BioGRID; 35464; 387. DR ComplexPortal; CPX-1732; Ku70:Ku80 complex. DR DIP; DIP-2483N; -. DR IntAct; P32807; 28. DR MINT; P32807; -. DR STRING; 4932.YMR284W; -. DR iPTMnet; P32807; -. DR MaxQB; P32807; -. DR PaxDb; 4932-YMR284W; -. DR PeptideAtlas; P32807; -. DR EnsemblFungi; YMR284W_mRNA; YMR284W; YMR284W. DR GeneID; 855328; -. DR KEGG; sce:YMR284W; -. DR AGR; SGD:S000004897; -. DR SGD; S000004897; YKU70. DR VEuPathDB; FungiDB:YMR284W; -. DR eggNOG; KOG2327; Eukaryota. DR GeneTree; ENSGT00940000153239; -. DR HOGENOM; CLU_024202_0_0_1; -. DR InParanoid; P32807; -. DR OMA; FWANVKH; -. DR OrthoDB; 21093at2759; -. DR BioCyc; YEAST:G3O-32954-MONOMER; -. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 855328; 0 hits in 10 CRISPR screens. DR PRO; PR:P32807; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P32807; Protein. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0043564; C:Ku70:Ku80 complex; IDA:SGD. DR GO; GO:0005635; C:nuclear envelope; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0070034; F:telomerase RNA binding; IDA:SGD. DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central. DR GO; GO:0006325; P:chromatin organization; IDA:SGD. DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD. DR GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IMP:SGD. DR GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IMP:SGD. DR GO; GO:0000725; P:recombinational repair; NAS:ComplexPortal. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR GO; GO:0000723; P:telomere maintenance; IMP:SGD. DR CDD; cd00788; KU70; 1. DR CDD; cd01458; vWA_ku; 1. DR Gene3D; 1.10.1600.10; -; 1. DR Gene3D; 2.40.290.10; -; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR InterPro; IPR006165; Ku70. DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom. DR InterPro; IPR047087; KU70_core_dom. DR InterPro; IPR005160; Ku_C. DR InterPro; IPR005161; Ku_N. DR InterPro; IPR016194; SPOC-like_C_dom_sf. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1. DR PANTHER; PTHR12604:SF2; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 6; 1. DR Pfam; PF02735; Ku; 1. DR Pfam; PF03730; Ku_C; 1. DR Pfam; PF03731; Ku_N; 1. DR PIRSF; PIRSF003033; Ku70; 1. DR SMART; SM00559; Ku78; 1. DR SUPFAM; SSF100939; SPOC domain-like; 1. DR SUPFAM; SSF53300; vWA-like; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chromosome; Direct protein sequencing; KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Telomere; Ubl conjugation. FT CHAIN 1..602 FT /note="ATP-dependent DNA helicase II subunit 1" FT /id="PRO_0000210184" FT DOMAIN 268..483 FT /note="Ku" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT VARIANT 21 FT /note="T -> K (in strain: ABYS 60 and SK1)" FT VARIANT 50 FT /note="E -> D (in strain: ABYS 60, DBVPG6044, SK1 and FT YPS128)" FT VARIANT 230 FT /note="T -> A (in strain: DBVPG6044)" FT VARIANT 368 FT /note="F -> I (in strain: YPS128)" FT VARIANT 562 FT /note="I -> T (in strain: ABYS 60, DBVPG6044, SK1 and FT YPS128)" FT CONFLICT 3 FT /note="S -> P (in Ref. 1; CAA49840)" FT /evidence="ECO:0000305" FT CONFLICT 87 FT /note="R -> T (in Ref. 4; AAT92882)" FT /evidence="ECO:0000305" FT STRAND 30..37 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 54..72 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 75..84 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 105..119 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 125..129 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 142..152 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 164..172 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 201..209 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 218..224 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 266..275 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 280..290 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 308..319 FT /evidence="ECO:0007829|PDB:5Y58" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 346..354 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 362..370 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 385..389 FT /evidence="ECO:0007829|PDB:5Y58" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 397..410 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 413..425 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 428..434 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:5Y58" FT STRAND 443..449 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 452..454 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 471..486 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 502..515 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 528..538 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 540..557 FT /evidence="ECO:0007829|PDB:5Y58" FT TURN 561..564 FT /evidence="ECO:0007829|PDB:5Y58" FT HELIX 565..583 FT /evidence="ECO:0007829|PDB:5Y58" SQ SEQUENCE 602 AA; 70647 MW; BD58160328EE6C6E CRC64; MRSVTNAFGN SGELNDQVDE TGYRKFDIHE GILFCIELSE TMFKESSDLE YKSPLLEILE SLDELMSQLV ITRPGTAIGC YFYYCNREDA KEGIYELFPL RDINATFMKK LNDLLEDLSS GRISLYDYFM FQQTGSEKQV RLSVLFTFML DTFLEEIPGQ KQLSNKRVFL FTDIDKPQEA QDIDERARLR RLTIDLFDNK VNFATFFIGY ADKPFDNEFY SDILQLGSHT NENTGLDSEF DGPSTKPIDA KYIKSRILRK KEVKRIMFQC PLILDEKTNF IVGVKGYTMY THEKAGVRYK LVYEHEDIRQ EAYSKRKFLN PITGEDVTGK TVKVYPYGDL DINLSDSQDQ IVMEAYTQKD AFLKIIGFRS SSKSIHYFNN IDKSSFIVPD EAKYEGSIRT LASLLKILRK KDKIAILWGK LKSNSHPSLY TLSPSSVKDY NEGFYLYRVP FLDEIRKFPS LLSYDDGSEH KLDYDNMKKV TQSIMGYFNL RDGYNPSDFK NPLLQKHYKV LHDYLLQIET TFDENETPNT KKDRMMREDD SLRKLYYIRN KILESEKSED PIIQRLNKYV KIWNMFYKKF NDDNISIKEE KKPFDKKPKF NI //