FRDA_YEAST
ID FRDA_YEAST Reviewed; 174 AA.
AC Q07540; D6VRN0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Frataxin homolog, mitochondrial;
DE EC=1.16.3.1;
DE Contains:
DE RecName: Full=Frataxin homolog intermediate form;
DE Flags: Precursor;
GN Name=YFH1; OrderedLocusNames=YDL120W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9180083; DOI=10.1126/science.276.5319.1709;
RA Babcock M., de Silva D., Oaks R., Davis-Kaplan S., Jiralerspong S.,
RA Montermini L., Pandolfo M., Kaplan J.;
RT "Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog
RT of frataxin.";
RL Science 276:1709-1712(1997).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9988680; DOI=10.1074/jbc.274.8.4497;
RA Radisky D.C., Babcock M.C., Kaplan J.;
RT "The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence
RT for a mitochondrial iron cycle.";
RL J. Biol. Chem. 274:4497-4499(1999).
RN [6]
RP PROCESSING.
RX PubMed=10545606; DOI=10.1093/hmg/8.12.2255;
RA Gordon D.M., Shi Q., Dancis A., Pain D.;
RT "Maturation of frataxin within mammalian and yeast mitochondria: one-step
RT processing by matrix processing peptidase.";
RL Hum. Mol. Genet. 8:2255-2262(1999).
RN [7]
RP PROCESSING.
RX PubMed=10428860; DOI=10.1074/jbc.274.32.22763;
RA Branda S.S., Cavadini P., Adamec J., Kalousek F., Taroni F., Isaya G.;
RT "Yeast and human frataxin are processed to mature form in two sequential
RT steps by the mitochondrial processing peptidase.";
RL J. Biol. Chem. 274:22763-22769(1999).
RN [8]
RP INTERACTION WITH ISU1.
RX PubMed=10588895; DOI=10.1006/jmbi.1999.3294;
RA Garland S.A., Hoff K., Vickery L.E., Culotta V.C.;
RT "Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene
RT family for iron-sulfur cluster assembly.";
RL J. Mol. Biol. 294:897-907(1999).
RN [9]
RP INTERACTION WITH ISU1.
RX PubMed=12947415; DOI=10.1038/sj.embor.embor918;
RA Gerber J., Muhlenhoff U., Lill R.;
RT "An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S
RT cluster synthesis on Isu1.";
RL EMBO Rep. 4:906-911(2003).
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, AND INTERACTION WITH YHB1; SDH1; SDH2; AIM45 AND CIR1.
RX PubMed=15961414; DOI=10.1093/hmg/ddi214;
RA Gonzalez-Cabo P., Vazquez-Manrique R.P., Garcia-Gimeno M.A., Sanz P.,
RA Palau F.;
RT "Frataxin interacts functionally with mitochondrial electron transport
RT chain proteins.";
RL Hum. Mol. Genet. 14:2091-2098(2005).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-79; ASP-82; GLU-93;
RP ASP-97 AND GLU-103.
RX PubMed=16371422; DOI=10.1093/hmg/ddi461;
RA Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., Isaya G.;
RT "Mitochondrial iron detoxification is a primary function of frataxin that
RT limits oxidative damage and preserves cell longevity.";
RL Hum. Mol. Genet. 15:467-479(2006).
RN [13]
RP INTERACTION WITH ISU1, AND MUTAGENESIS OF 122-ASN--GLU-124.
RX PubMed=18319250; DOI=10.1074/jbc.m800399200;
RA Wang T., Craig E.A.;
RT "Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis,
RT Isu.";
RL J. Biol. Chem. 283:12674-12679(2008).
RN [14]
RP FUNCTION IN IRON-SULFUR CLUSTER BIOSYNTHESIS, INTERACTION WITH ISU1, AND
RP MUTAGENESIS OF GLN-129; ILE-130; TRP-131 AND ARG-141.
RX PubMed=19884169; DOI=10.1093/hmg/ddp495;
RA Leidgens S., De Smet S., Foury F.;
RT "Frataxin interacts with Isu1 through a conserved tryptophan in its beta-
RT sheet.";
RL Hum. Mol. Genet. 19:276-286(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 52-174 ALONE AND IN COMPLEX WITH
RP IRON, ELECTRON MICROSCOPY OF MUTANT ALA-73, FUNCTION, AND SUBUNIT.
RX PubMed=17027502; DOI=10.1016/j.str.2006.08.010;
RA Karlberg T., Schagerlof U., Gakh O., Park S., Ryde U., Lindahl M.,
RA Leath K., Garman E., Isaya G., Al-Karadaghi S.;
RT "The structures of frataxin oligomers reveal the mechanism for the delivery
RT and detoxification of iron.";
RL Structure 14:1535-1546(2006).
RN [16]
RP ELECTRON MICROSCOPY OF MUTANT ALA-73 (13 ANGSTROMS), AND SUBUNIT.
RX PubMed=18393441; DOI=10.1021/bi800052m;
RA Schagerlof U., Elmlund H., Gakh O., Nordlund G., Hebert H., Lindahl M.,
RA Isaya G., Al-Karadaghi S.;
RT "Structural basis of the iron storage function of frataxin from single-
RT particle reconstruction of the iron-loaded oligomer.";
RL Biochemistry 47:4948-4954(2008).
CC -!- FUNCTION: Promotes the biosynthesis of heme as well as the assembly and
CC repair of iron-sulfur clusters by delivering Fe(2+) to proteins
CC involved in these pathways. Plays a role in the protection against
CC iron-catalyzed oxidative stress through its ability to catalyze the
CC oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in
CC the form of a ferrihydrite mineral by oligomerization. May be involved
CC in regulation of the mitochondrial electron transport chain.
CC {ECO:0000269|PubMed:15961414, ECO:0000269|PubMed:16371422,
CC ECO:0000269|PubMed:17027502, ECO:0000269|PubMed:19884169,
CC ECO:0000269|PubMed:9180083, ECO:0000269|PubMed:9988680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000269|PubMed:16371422};
CC -!- SUBUNIT: Monomer; increments in mitochondrial iron uptake induce
CC stepwise assembly of species ranging from trimers to 24-mers. Interacts
CC with ISU1. Interacts with YHB1, SDH1, SDH2, AIM45 and CIR1.
CC {ECO:0000269|PubMed:10588895, ECO:0000269|PubMed:12947415,
CC ECO:0000269|PubMed:15961414, ECO:0000269|PubMed:17027502,
CC ECO:0000269|PubMed:18319250, ECO:0000269|PubMed:18393441,
CC ECO:0000269|PubMed:19884169}.
CC -!- INTERACTION:
CC Q07540; Q03020: ISU1; NbExp=4; IntAct=EBI-2206814, EBI-29901;
CC Q07540; Q07540: YFH1; NbExp=2; IntAct=EBI-2206814, EBI-2206814;
CC Q07540; P39676: YHB1; NbExp=2; IntAct=EBI-2206814, EBI-6905;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9180083,
CC ECO:0000269|PubMed:9988680}.
CC -!- PTM: Processed in two steps by mitochondrial processing peptidase
CC (MPP). MPP first cleaves the precursor to intermediate form and
CC subsequently converts the intermediate to mature size protein.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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DR EMBL; Z74168; CAA98688.1; -; Genomic_DNA.
DR EMBL; AY558160; AAS56486.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11740.1; -; Genomic_DNA.
DR PIR; S67663; S67663.
DR RefSeq; NP_010163.1; NM_001180179.1.
DR PDB; 2FQL; X-ray; 3.01 A; A=52-174.
DR PDB; 2GA5; NMR; -; A=53-174.
DR PDB; 3OEQ; X-ray; 2.96 A; A=52-174.
DR PDB; 3OER; X-ray; 3.20 A; A=52-174.
DR PDB; 4EC2; X-ray; 3.00 A; A=52-174.
DR PDB; 5T0V; EM; 17.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=52-172.
DR PDB; 5TRE; EM; 15.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=52-172.
DR PDBsum; 2FQL; -.
DR PDBsum; 2GA5; -.
DR PDBsum; 3OEQ; -.
DR PDBsum; 3OER; -.
DR PDBsum; 4EC2; -.
DR PDBsum; 5T0V; -.
DR PDBsum; 5TRE; -.
DR AlphaFoldDB; Q07540; -.
DR BMRB; Q07540; -.
DR SASBDB; Q07540; -.
DR SMR; Q07540; -.
DR BioGRID; 31943; 111.
DR ComplexPortal; CPX-392; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR DIP; DIP-7485N; -.
DR IntAct; Q07540; 11.
DR MINT; Q07540; -.
DR STRING; 4932.YDL120W; -.
DR TCDB; 9.B.21.1.2; the frataxin (frataxin) family.
DR MaxQB; Q07540; -.
DR PaxDb; Q07540; -.
DR PRIDE; Q07540; -.
DR EnsemblFungi; YDL120W_mRNA; YDL120W; YDL120W.
DR GeneID; 851437; -.
DR KEGG; sce:YDL120W; -.
DR SGD; S000002278; YFH1.
DR VEuPathDB; FungiDB:YDL120W; -.
DR eggNOG; KOG3413; Eukaryota.
DR GeneTree; ENSGT00390000005811; -.
DR HOGENOM; CLU_080880_2_4_1; -.
DR InParanoid; Q07540; -.
DR OMA; FYKNEWI; -.
DR BioCyc; MetaCyc:G3O-29519-MON; -.
DR BioCyc; YEAST:G3O-29519-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR SABIO-RK; Q07540; -.
DR EvolutionaryTrace; Q07540; -.
DR PRO; PR:Q07540; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07540; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IDA:SGD.
DR GO; GO:0004322; F:ferroxidase activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0034986; F:iron chaperone activity; IDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IMP:UniProtKB.
DR GO; GO:0010040; P:response to iron(II) ion; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR Gene3D; 3.30.920.10; -; 1.
DR InterPro; IPR017789; Frataxin.
DR InterPro; IPR002908; Frataxin/CyaY.
DR InterPro; IPR036524; Frataxin/CyaY_sf.
DR InterPro; IPR020895; Frataxin_CS.
DR PANTHER; PTHR16821; PTHR16821; 1.
DR Pfam; PF01491; Frataxin_Cyay; 1.
DR SMART; SM01219; Frataxin_Cyay; 1.
DR SUPFAM; SSF55387; SSF55387; 1.
DR TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR TIGRFAMs; TIGR03422; mito_frataxin; 1.
DR PROSITE; PS01344; FRATAXIN_1; 1.
DR PROSITE; PS50810; FRATAXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme biosynthesis; Ion transport; Iron; Iron storage;
KW Iron transport; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 22..174
FT /note="Frataxin homolog intermediate form"
FT /id="PRO_0000010135"
FT CHAIN 52..174
FT /note="Frataxin homolog, mitochondrial"
FT /id="PRO_0000010136"
FT MUTAGEN 79
FT /note="D->A: Nearly abolishes ferroxidase activity, slows
FT down oligomerization, impairs resistance to iron-catalyzed
FT oxidative stress, no effect on Fe(2+) delivery and cell
FT growth; when associated with A-82."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 82
FT /note="D->A: Nearly abolishes ferroxidase activity, slows
FT down oligomerization, impairs resistance to iron-catalyzed
FT oxidative stress, no effect on Fe(2+) delivery and cell
FT growth; when associated with A-79."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 93
FT /note="E->A: Impairs oligomerization and iron
FT mineralization."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 93
FT /note="E->A: Impairs resistance to iron-catalyzed oxidative
FT stress, no effect on Fe(2+) delivery and cell growth; when
FT associated with A-97 and A-103."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 97
FT /note="D->A: Impairs resistance to iron-catalyzed oxidative
FT stress, no effect on Fe(2+) delivery and cell growth; when
FT associated with A-93 and A-103."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 103
FT /note="E->A: Impairs resistance to iron-catalyzed oxidative
FT stress, no effect on Fe(2+) delivery and cell growth; when
FT associated with A-93 and A-97."
FT /evidence="ECO:0000269|PubMed:16371422"
FT MUTAGEN 122..124
FT /note="NKQ->ATA: Impairs cell growth, lowers activity of
FT mitochondrial iron-sulfur cluster-containing enzymes, no
FT effect on iron binding and oligomerization."
FT /evidence="ECO:0000269|PubMed:18319250"
FT MUTAGEN 129
FT /note="Q->A: Impairs cell growth and lowers aconitase
FT activity."
FT /evidence="ECO:0000269|PubMed:19884169"
FT MUTAGEN 130
FT /note="I->A: Impairs cell growth and lowers aconitase
FT activity."
FT /evidence="ECO:0000269|PubMed:19884169"
FT MUTAGEN 131
FT /note="W->A: Impairs cell growth, lowers aconitase activity
FT and strongly decreases interaction with ISU1."
FT /evidence="ECO:0000269|PubMed:19884169"
FT MUTAGEN 131
FT /note="W->F: Lowers aconitase activity and no effexct on
FT interaction with ISU1."
FT /evidence="ECO:0000269|PubMed:19884169"
FT MUTAGEN 141
FT /note="R->A: Impairs cell growth and lowers aconitase
FT activity."
FT /evidence="ECO:0000269|PubMed:19884169"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3OEQ"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:3OEQ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2FQL"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3OEQ"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3OEQ"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3OEQ"
FT STRAND 138..151
FT /evidence="ECO:0007829|PDB:3OEQ"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3OEQ"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:3OEQ"
SQ SEQUENCE 174 AA; 19490 MW; AB1FF7478EF0E5D6 CRC64;
MIKRSLASLV RVSSVMGRRY MIAAAGGERA RFCPAVTNKK NHTVNTFQKR FVESSTDGQV
VPQEVLNLPL EKYHEEADDY LDHLLDSLEE LSEAHPDCIP DVELSHGVMT LEIPAFGTYV
INKQPPNKQI WLASPLSGPN RFDLLNGEWV SLRNGTKLTD ILTEEVEKAI SKSQ
