LONM_YEAST
ID LONM_YEAST Reviewed; 1133 AA.
AC P36775; D6VPX8; P13435;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120}; Synonyms=LON;
GN OrderedLocusNames=YBL022C; ORFNames=YBL0440;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8276800; DOI=10.1016/s0021-9258(17)42340-4;
RA van Dyck L., Pearce D.A., Sherman F.;
RT "PIM1 encodes a mitochondrial ATP-dependent protease that is required for
RT mitochondrial function in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:238-242(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8146662; DOI=10.1126/science.8146662;
RA Suzuki C.K., Suda K., Wang N., Schatz G.;
RT "Requirement for the yeast gene LON in intramitochondrial proteolysis and
RT maintenance of respiration.";
RL Science 264:273-276(1994).
RN [3]
RP ERRATUM OF PUBMED:8146662.
RX PubMed=8178144; DOI=10.1126/science.8178144;
RA Suzuki C.K., Suda K., Wang N., Schatz G.;
RL Science 264:891-891(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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] OF 1-216.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=2832732; DOI=10.1128/mcb.8.2.655-663.1988;
RA Hahn S., Pinkham J., Wei R., Miller R., Guarente L.;
RT "The HAP3 regulatory locus of Saccharomyces cerevisiae encodes divergent
RT overlapping transcripts.";
RL Mol. Cell. Biol. 8:655-663(1988).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MUTAGENESIS OF LYS-638 AND
RP SER-1015, AUTOCATALYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=9405361; DOI=10.1093/emboj/16.24.7317;
RA Wagner I., van Dyck L., Savel'ev A.S., Neupert W., Langer T.;
RT "Autocatalytic processing of the ATP-dependent PIM1 protease: crucial
RT function of a pro-region for sorting to mitochondria.";
RL EMBO J. 16:7317-7325(1997).
RN [8]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBUNIT.
RX PubMed=9724747; DOI=10.1073/pnas.95.18.10584;
RA van Dijl J.M., Kutejova E., Suda K., Perecko D., Schatz G., Suzuki C.K.;
RT "The ATPase and protease domains of yeast mitochondrial Lon: roles in
RT proteolysis and respiration-dependent growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10584-10589(1998).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8354406; DOI=10.1016/0014-5793(93)80190-6;
RA Kutejova E., Durcova G., Surovkova E., Kuzela S.;
RT "Yeast mitochondrial ATP-dependent protease: purification and comparison
RT with the homologous rat enzyme and the bacterial ATP-dependent protease
RT La.";
RL FEBS Lett. 329:47-50(1993).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF LYS-638 AND SER-1015.
RX PubMed=8810243; DOI=10.1126/science.274.5284.103;
RA Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.;
RT "Promotion of mitochondrial membrane complex assembly by a proteolytically
RT inactive yeast Lon.";
RL Science 274:103-106(1996).
RN [11]
RP ERRATUM OF PUBMED:8810243.
RX DOI=10.1126/science.275.5301.737f;
RA Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.;
RL Science 275:741-741(1997).
RN [12]
RP SUBUNIT.
RX PubMed=10359790; DOI=10.1073/pnas.96.12.6787;
RA Stahlberg H., Kutejova E., Suda K., Wolpensinger B., Lustig A., Schatz G.,
RA Engel A., Suzuki C.K.;
RT "Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease
RT with seven flexible subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6787-6790(1999).
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 FUNCTION.
RX PubMed=15870080; DOI=10.1074/jbc.m502796200;
RA Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D.,
RA Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.;
RT "Cleavage site selection within a folded substrate by the ATP-dependent lon
RT protease.";
RL J. Biol. Chem. 280:25103-25110(2005).
RN [16]
RP FUNCTION, AND SUBSTRATE.
RX PubMed=16428434; DOI=10.1128/mcb.26.3.762-776.2006;
RA Major T., von Janowsky B., Ruppert T., Mogk A., Voos W.;
RT "Proteomic analysis of mitochondrial protein turnover: identification of
RT novel substrate proteins of the matrix protease pim1.";
RL Mol. Cell. Biol. 26:762-776(2006).
RN [17]
RP SUBSTRATE.
RX PubMed=20150421; DOI=10.1074/jbc.m109.065425;
RA Bayot A., Gareil M., Rogowska-Wrzesinska A., Roepstorff P., Friguet B.,
RA Bulteau A.L.;
RT "Identification of novel oxidized protein substrates and physiological
RT partners of the mitochondrial ATP-dependent Lon-like protease Pim1.";
RL J. Biol. Chem. 285:11445-11457(2010).
RN [18]
RP SUBSTRATE.
RX PubMed=28377575; DOI=10.1038/s41598-017-00632-8;
RA Kunova N., Ondrovicova G., Bauer J.A., Bellova J., Ambro L.,
RA Martinakova L., Kotrasova V., Kutejova E., Pevala V.;
RT "The role of Lon-mediated proteolysis in the dynamics of mitochondrial
RT nucleic acid-protein complexes.";
RL Sci. Rep. 7:631-631(2017).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC in a site-specific manner (PubMed:15870080, PubMed:16428434,
CC PubMed:8146662, PubMed:8276800, PubMed:8354406, PubMed:8810243,
CC PubMed:9405361, PubMed:9724747). Endogenous substrates include ABF2,
CC ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized proteins. The
CC 2 nucleic acid-binding proteins ABF2 and MGM101 are protected from
CC degradation by PIM1 when they are bound to DNA (PubMed:16428434,
CC PubMed:20150421, PubMed:28377575). {ECO:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:16428434,
CC ECO:0000269|PubMed:20150421, ECO:0000269|PubMed:28377575,
CC ECO:0000269|PubMed:8146662, ECO:0000269|PubMed:8276800,
CC ECO:0000269|PubMed:8354406, ECO:0000269|PubMed:8810243,
CC ECO:0000269|PubMed:9405361, ECO:0000269|PubMed:9724747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for ATP for ATPase activity {ECO:0000269|PubMed:8354406};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:8354406};
CC -!- SUBUNIT: Homoheptamer. Organized in a ring with a central cavity.
CC Oligomerization is independent of its proteolytic activity and the
CC autocatalytic maturation of its subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:10359790,
CC ECO:0000269|PubMed:9724747}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9405361}.
CC -!- MISCELLANEOUS: Present with 14500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; X74544; CAA52634.1; -; Genomic_DNA.
DR EMBL; L28110; AAA53625.1; -; mRNA.
DR EMBL; Z35783; CAA84841.1; -; Genomic_DNA.
DR EMBL; M20318; AAA53539.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07098.1; -; Genomic_DNA.
DR PIR; S43938; S43938.
DR RefSeq; NP_009531.1; NM_001178262.1.
DR PDB; 7SXO; EM; 3.30 A; A/B/C/D/E/F=182-1133.
DR PDBsum; 7SXO; -.
DR AlphaFoldDB; P36775; -.
DR SMR; P36775; -.
DR BioGRID; 32676; 113.
DR DIP; DIP-6629N; -.
DR IntAct; P36775; 16.
DR STRING; 4932.YBL022C; -.
DR MEROPS; S16.010; -.
DR iPTMnet; P36775; -.
DR MaxQB; P36775; -.
DR PaxDb; P36775; -.
DR PRIDE; P36775; -.
DR EnsemblFungi; YBL022C_mRNA; YBL022C; YBL022C.
DR GeneID; 852259; -.
DR KEGG; sce:YBL022C; -.
DR SGD; S000000118; PIM1.
DR VEuPathDB; FungiDB:YBL022C; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; P36775; -.
DR OMA; YVGPPIY; -.
DR BioCyc; YEAST:G3O-28925-MON; -.
DR BRENDA; 3.4.21.53; 984.
DR PRO; PR:P36775; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P36775; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IMP:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IGI:SGD.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; TAS:AgBase.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; TAS:AgBase.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; TAS:AgBase.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:SGD.
DR GO; GO:1901858; P:regulation of mitochondrial DNA metabolic process; IMP:SGD.
DR GO; GO:0009408; P:response to heat; TAS:AgBase.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03120; lonm_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027503; Lonm_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43718; PTHR43718; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW Hydrolase; Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Serine protease; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT PROPEP 38..98
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120,
FT ECO:0000269|PubMed:9405361, ECO:0000269|PubMed:9724747"
FT /id="PRO_0000395761"
FT CHAIN 99..1133
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000026733"
FT DOMAIN 182..478
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 923..1109
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 98..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1015
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 1058
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 632..639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT MUTAGEN 638
FT /note="K->N: Abolishes ATP-binding."
FT /evidence="ECO:0000269|PubMed:8810243,
FT ECO:0000269|PubMed:9405361"
FT MUTAGEN 1015
FT /note="S->A: Abolishes peptidase activity."
FT /evidence="ECO:0000269|PubMed:8810243,
FT ECO:0000269|PubMed:9405361"
FT CONFLICT 509
FT /note="Q -> R (in Ref. 2; AAA53625)"
FT /evidence="ECO:0000305"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 541..555
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 562..576
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 589..599
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 604..618
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:7SXO"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 641..648
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 713..721
FT /evidence="ECO:0007829|PDB:7SXO"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 743..750
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 757..762
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 773..791
FT /evidence="ECO:0007829|PDB:7SXO"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 803..812
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 820..839
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:7SXO"
FT TURN 903..906
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 907..910
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 928..935
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 938..949
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 967..988
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 994..996
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1000..1003
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1017..1029
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1037..1039
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1048..1050
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1055..1064
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1068..1073
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1074..1076
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1077..1082
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1085..1088
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1092..1098
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1099..1106
FT /evidence="ECO:0007829|PDB:7SXO"
FT TURN 1112..1114
FT /evidence="ECO:0007829|PDB:7SXO"
FT STRAND 1115..1119
FT /evidence="ECO:0007829|PDB:7SXO"
FT HELIX 1120..1128
FT /evidence="ECO:0007829|PDB:7SXO"
SQ SEQUENCE 1133 AA; 127112 MW; 281CAB94579FFF09 CRC64;
MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK PSHIIKSPTW
QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD DSTSQKKDED VKIVPDEKDT
DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP
QMLALPIARR PLFPGFYKAV VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK
NDVYDVGVLA QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT
DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE ESEELDDIQE
GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS EILKVFKEIS QLNTMFREQI
ATFSASIQSA TTNIFEEPAR LADFAAAVSA GEEDELQDIL SSLNIEHRLE KSLLVLKKEL
MNAELQNKIS KDVETKIQKR QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP
DSVQKIFDDE ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH
YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN RKFFRFSVGG
MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE IDKIGHGGIH GDPSAALLEV
LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN SLETIPRPLL DRMEVIELTG YVAEDKVKIA
EQYLVPSAKK SAGLENSHVD MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK
LSIEDSPTSS ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS
ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ PLHNCKHPTF
ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI HLHCPEGATP KDGPSAGVTM
ATSFLSLALN KSIDPTVAMT GELTLTGKVL RIGGLREKAV AAKRSGAKTI IFPKDNLNDW
EELPDNVKEG LEPLAADWYN DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD
