ID   BLH1_YEAST              Reviewed;         483 AA.
AC   Q01532; D6W0V4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 3.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Cysteine proteinase 1, mitochondrial;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
DE            Short=BLM hydrolase;
DE   AltName: Full=Homocysteine-thiolactonase;
DE            Short=HTLase;
DE            Short=Hcy-thiolactonase;
DE   AltName: Full=Leucine aminopeptidase 3;
DE   AltName: Full=Y3;
DE   Flags: Precursor;
GN   Name=LAP3; Synonyms=BLH1, GAL6, YCP1; OrderedLocusNames=YNL239W;
GN   ORFNames=N1118;
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], BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RX   PubMed=1400467; DOI=10.1016/s0021-9258(19)36648-7;
RA   Kambouris N.G., Burke D.J., Creutz C.E.;
RT   "Cloning and characterization of a cysteine proteinase from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 267:21570-21576(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 228-250 AND
RP   367-387.
RX   PubMed=8424954; DOI=10.1016/0167-4781(93)90069-p;
RA   Magdolen U., Mueller G., Magdolen V., Bandlow W.;
RT   "A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate
RT   bleomycin hydrolase, a family member of thiol proteinases.";
RL   Biochim. Biophys. Acta 1171:299-303(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RX   PubMed=8463237; DOI=10.1016/s0021-9258(18)53142-2;
RA   Enenkel C., Wolf D.H.;
RT   "BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian
RT   bleomycin hydrolase.";
RL   J. Biol. Chem. 268:7036-7043(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8896273;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA   Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT   "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT   reading frames including a novel gene encoding a globin-like domain.";
RL   Yeast 12:1071-1076(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, MASS SPECTROMETRY, AND
RP   MUTAGENESIS OF CYS-102 AND 271-LYS--LYS-274.
RX   PubMed=9374524; DOI=10.1074/jbc.272.48.30350;
RA   Zheng W., Xu H.E., Johnston S.A.;
RT   "The cysteine-peptidase bleomycin hydrolase is a member of the galactose
RT   regulon in yeast.";
RL   J. Biol. Chem. 272:30350-30355(1997).
RN   [8]
RP   PROTEIN SEQUENCE OF 228-251 AND 367-387.
RX   PubMed=1882548; DOI=10.1002/yea.320070305;
RA   Creutz C.E., Snyder S.L., Kambouris N.G.;
RT   "Calcium-dependent secretory vesicle-binding and lipid-binding proteins of
RT   Saccharomyces cerevisiae.";
RL   Yeast 7:229-244(1991).
RN   [9]
RP   PROTEIN SEQUENCE OF C-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF
RP   30-483, AND SUBUNIT.
RX   PubMed=7638617; DOI=10.1126/science.7638617;
RA   Joshua-Tor L., Xu H.E., Johnston S.A., Rees D.C.;
RT   "Crystal structure of a conserved protease that binds DNA: the bleomycin
RT   hydrolase, Gal6.";
RL   Science 269:945-950(1995).
RN   [10]
RP   DNA-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8063738; DOI=10.1016/s0021-9258(17)31945-2;
RA   Xu H.E., Johnston S.A.;
RT   "Yeast bleomycin hydrolase is a DNA-binding cysteine protease.
RT   Identification, purification, biochemical characterization.";
RL   J. Biol. Chem. 269:21177-21183(1994).
RN   [11]
RP   DNA-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=9584198; DOI=10.1128/mcb.18.6.3580;
RA   Zheng W., Johnston S.A.;
RT   "The nucleic acid binding activity of bleomycin hydrolase is involved in
RT   bleomycin detoxification.";
RL   Mol. Cell. Biol. 18:3580-3585(1998).
RN   [12]
RP   FUNCTION.
RX   PubMed=12555812; DOI=10.1139/o02-167;
RA   Wang H., Ramotar D.;
RT   "Cellular resistance to bleomycin in Saccharomyces cerevisiae is not
RT   affected by changes in bleomycin hydrolase levels.";
RL   Biochem. Cell Biol. 80:789-796(2002).
RN   [13]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [14]
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   [15]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [16]
RP   FUNCTION, AND MUTAGENESIS OF HIS-398.
RX   PubMed=16769724; DOI=10.1074/jbc.m603656200;
RA   Zimny J., Sikora M., Guranowski A., Jakubowski H.;
RT   "Protective mechanisms against homocysteine toxicity: the role of bleomycin
RT   hydrolase.";
RL   J. Biol. Chem. 281:22485-22492(2006).
RN   [17]
RP   ALTERNATIVE INITIATION.
RX   PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA   Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA   Ito T.;
RT   "A large-scale full-length cDNA analysis to explore the budding yeast
RT   transcriptome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 30-483 OF MUTANT ALA-102, AND
RP   MUTAGENESIS OF GLY-479.
RX   PubMed=9546396; DOI=10.1016/s0092-8674(00)81150-2;
RA   Zheng W., Johnston S.A., Joshua-Tor L.;
RT   "The unusual active site of Gal6/bleomycin hydrolase can act as a
RT   carboxypeptidase, aminopeptidase, and peptide ligase.";
RL   Cell 93:103-109(1998).
CC   -!- FUNCTION: The normal physiological role of the enzyme is unknown, but
CC       it is not essential for the viability of yeast cells. Has
CC       aminopeptidase activity, shortening substrate peptides sequentially by
CC       1 amino acid. Has bleomycin hydrolase activity, which can protect the
CC       cell from the toxic effects of bleomycin. Has homocysteine-
CC       thiolactonase activity, protecting the cell against homocysteine
CC       toxicity. Acts as a repressor in the GAL4 regulatory system, but this
CC       does not require either the peptidase or nucleic acid-binding
CC       activities. {ECO:0000269|PubMed:12555812, ECO:0000269|PubMed:16769724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
CC         hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
CC         shows general aminopeptidase activity. The specificity varies
CC         somewhat with source, but amino acid arylamides of Met, Leu and Ala
CC         are preferred.; EC=3.4.22.40;
CC   -!- ACTIVITY REGULATION: Inhibited by E64, a specific inhibitor of cysteine
CC       proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions.
CC       {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8463237}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.8 uM for arginine-4-methyl-7-coumarylamide
CC         {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738,
CC         ECO:0000269|PubMed:8463237};
CC         KM=0.33 mM for glutamine-beta-naphthylamide
CC         {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738,
CC         ECO:0000269|PubMed:8463237};
CC         KM=228 uM for lysine-4-methyl-7-coumarylamide
CC         {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738,
CC         ECO:0000269|PubMed:8463237};
CC         Vmax=2.56 umol/h/mg enzyme for arginine-4-methyl-7-coumarylamide
CC         {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738,
CC         ECO:0000269|PubMed:8463237};
CC         Vmax=370 nmol/min/mg enzyme for glutamine-beta-naphthylamide
CC         {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738,
CC         ECO:0000269|PubMed:8463237};
CC         Note=N-terminal acetylation of lysine-4-methyl-7-coumarylamide
CC         (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this
CC         substrate.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:1400467,
CC         ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237};
CC   -!- SUBUNIT: Homohexamer. Binds to nucleic acids. Binds single-stranded DNA
CC       and RNA with higher affinity than double-stranded DNA.
CC       {ECO:0000269|PubMed:7638617}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=Q01532-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=Q01532-2; Sequence=VSP_026453;
CC   -!- PTM: The N-terminus of isoform Cytoplasmic is blocked.
CC   -!- MASS SPECTROMETRY: Mass=51830; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9374524};
CC   -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: [Isoform Cytoplasmic]: Produced by alternative
CC       initiation at Met-30 of isoform Mitochondrial. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   EMBL; M97910; AAA35231.1; -; Genomic_DNA.
DR   EMBL; X69124; CAA48878.1; -; Genomic_DNA.
DR   EMBL; X68228; CAA48309.1; -; Genomic_DNA.
DR   EMBL; Z71515; CAA96144.1; -; Genomic_DNA.
DR   EMBL; Z69381; CAA93359.1; -; Genomic_DNA.
DR   EMBL; U74299; AAB18260.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10320.1; -; Genomic_DNA.
DR   PIR; A46093; S25606.
DR   RefSeq; NP_014160.2; NM_001183077.1. [Q01532-2]
DR   PDB; 1A6R; X-ray; 2.05 A; A=32-483.
DR   PDB; 1GCB; X-ray; 2.20 A; A=30-483.
DR   PDB; 2DZY; X-ray; 2.57 A; A=30-482.
DR   PDB; 2DZZ; X-ray; 2.15 A; A=30-482.
DR   PDB; 2E00; X-ray; 2.00 A; A=30-482.
DR   PDB; 2E01; X-ray; 1.73 A; A=30-482.
DR   PDB; 2E02; X-ray; 2.20 A; A=30-482.
DR   PDB; 2E03; X-ray; 2.13 A; A=30-482.
DR   PDB; 3GCB; X-ray; 1.87 A; A=30-482.
DR   PDBsum; 1A6R; -.
DR   PDBsum; 1GCB; -.
DR   PDBsum; 2DZY; -.
DR   PDBsum; 2DZZ; -.
DR   PDBsum; 2E00; -.
DR   PDBsum; 2E01; -.
DR   PDBsum; 2E02; -.
DR   PDBsum; 2E03; -.
DR   PDBsum; 3GCB; -.
DR   AlphaFoldDB; Q01532; -.
DR   SMR; Q01532; -.
DR   BioGRID; 35600; 54.
DR   DIP; DIP-2941N; -.
DR   IntAct; Q01532; 11.
DR   MINT; Q01532; -.
DR   STRING; 4932.YNL239W; -.
DR   MEROPS; C01.085; -.
DR   iPTMnet; Q01532; -.
DR   MaxQB; Q01532; -.
DR   PaxDb; 4932-YNL239W; -.
DR   PeptideAtlas; Q01532; -.
DR   EnsemblFungi; YNL239W_mRNA; YNL239W; YNL239W. [Q01532-2]
DR   GeneID; 855482; -.
DR   KEGG; sce:YNL239W; -.
DR   AGR; SGD:S000005183; -.
DR   SGD; S000005183; LAP3.
DR   eggNOG; KOG4128; Eukaryota.
DR   GeneTree; ENSGT00390000001735; -.
DR   HOGENOM; CLU_038600_0_1_1; -.
DR   InParanoid; Q01532; -.
DR   OMA; DDGGWWQ; -.
DR   OrthoDB; 45184at2759; -.
DR   BioCyc; YEAST:G3O-33237-MONOMER; -.
DR   BRENDA; 3.4.13.23; 984.
DR   BRENDA; 3.4.22.40; 984.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SABIO-RK; Q01532; -.
DR   BioGRID-ORCS; 855482; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q01532; -.
DR   PRO; PR:Q01532; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; Q01532; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:SGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR   GO; GO:0043418; P:homocysteine catabolic process; IDA:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IDA:SGD.
DR   GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
DR   CDD; cd00585; Peptidase_C1B; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR   PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Hydrolase; Mitochondrion; Protease; Reference proteome;
KW   Thiol protease; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..482
FT                   /note="Cysteine proteinase 1, mitochondrial"
FT                   /id="PRO_0000050554"
FT   PROPEP          483
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:7638617"
FT                   /id="PRO_0000292865"
FT   ACT_SITE        102
FT   ACT_SITE        398
FT   ACT_SITE        421
FT   VAR_SEQ         1..29
FT                   /note="Missing (in isoform Cytoplasmic)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_026453"
FT   MUTAGEN         102
FT                   /note="C->A: Abolishes peptidase activity, which also
FT                   hinders autocatalytic processing of the enzyme to the
FT                   mature form."
FT                   /evidence="ECO:0000269|PubMed:9374524"
FT   MUTAGEN         271..274
FT                   /note="KDKK->ADAA: In GAL6DB; disrupts nucleic acid-binding
FT                   activity, but retains normal peptidase activity."
FT                   /evidence="ECO:0000269|PubMed:9374524"
FT   MUTAGEN         398
FT                   /note="H->A: Abolishes Hcy-thiolactonase activity."
FT                   /evidence="ECO:0000269|PubMed:16769724"
FT   MUTAGEN         479
FT                   /note="G->A: Results in the abnormal cleavage of 3
FT                   C-terminal residues instead of only 1 during autocatalytic
FT                   processing."
FT                   /evidence="ECO:0000269|PubMed:9546396"
FT   CONFLICT        187
FT                   /note="I -> M (in Ref. 2; CAA48878)"
FT                   /evidence="ECO:0000305"
FT   HELIX           36..47
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           50..59
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           64..68
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:3GCB"
FT   HELIX           102..118
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           128..149
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           158..165
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           174..184
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           203..226
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:1A6R"
FT   HELIX           232..252
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          264..269
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          275..280
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           282..288
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           333..345
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          350..354
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   TURN            356..359
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   TURN            362..365
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           385..390
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          398..407
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   TURN            409..411
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          414..420
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   TURN            425..428
FT                   /evidence="ECO:0007829|PDB:2E03"
FT   STRAND          432..436
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           437..443
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          444..450
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           451..453
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           456..463
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   STRAND          470..472
FT                   /evidence="ECO:0007829|PDB:2E01"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:1A6R"
SQ   SEQUENCE   483 AA;  55483 MW;  BF92A6049F98DD3D CRC64;
     MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL THQLATTVLK
     NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG RCWLFAATNQ LRLNVLSELN
     LKEFELSQAY LFFYDKLEKA NYFLDQIVSS ADQDIDSRLV QYLLAAPTED GGQYSMFLNL
     VKKYGLIPKD LYGDLPYSTT ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ
     MQREIFRLMS LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL
     INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV FFGSHTPKFM
     DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM LITGCHVDET SKLPLRYRVE
     NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD INELPKELAS KFTSGKEEPI VLPIWDPMGA
     LAK
//