KU70_YEAST
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 03-AUG-2022, entry version 191.
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, DBVPG3051,
RC 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}.
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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; 365.
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; P32807; -.
DR PRIDE; P32807; -.
DR EnsemblFungi; YMR284W_mRNA; YMR284W; YMR284W.
DR GeneID; 855328; -.
DR KEGG; sce:YMR284W; -.
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; PNDMMGI; -.
DR BioCyc; YEAST:G3O-32954-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:UniProtKB-EC.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR GO; GO:0071481; P:cellular response to X-ray; 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; IC:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_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:SF2; PTHR12604:SF2; 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; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 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
