BLH1_YEAST
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 03-AUG-2022, entry version 197.
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 (Ac-
CC 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; 51.
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; Q01532; -.
DR PeptideAtlas; Q01532; -.
DR PRIDE; Q01532; -.
DR EnsemblFungi; YNL239W_mRNA; YNL239W; YNL239W. [Q01532-2]
DR GeneID; 855482; -.
DR KEGG; sce:YNL239W; -.
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 BioCyc; YEAST:G3O-33237-MON; -.
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 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: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 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; PTHR10363; 1.
DR Pfam; PF03051; Peptidase_C1_2; 1.
DR PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; SSF54001; 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 C-
FT 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
