ID   QRI7_YEAST              Reviewed;         407 AA.
AC   P43122; D6VRP6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 188.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:23620299};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein QRI7 {ECO:0000255|HAMAP-Rule:MF_03179};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein QRI7 {ECO:0000255|HAMAP-Rule:MF_03179};
DE   Flags: Precursor;
GN   Name=QRI7; OrderedLocusNames=YDL104C; ORFNames=D2366;
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].
RX   PubMed=7725801; DOI=10.1002/yea.320101215;
RA   Simon M., Benit P., Vassal A., Dubois C., Faye G.;
RT   "Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces
RT   cerevisiae.";
RL   Yeast 10:1653-1656(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896274;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1077::aid-yea8%3e3.0.co;2-z;
RA   Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT   "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT   cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT   genes, and six new open reading frames.";
RL   Yeast 12:1077-1084(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
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   [4]
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   [5]
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   [6]
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   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [8]
RP   FUNCTION IN MITOCHONDRIAL GENOME MAINTENANCE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19578062; DOI=10.1093/nar/gkp557;
RA   Oberto J., Breuil N., Hecker A., Farina F., Brochier-Armanet C.,
RA   Culetto E., Forterre P.;
RT   "Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein,
RT   is essential for mitochondrial genome maintenance.";
RL   Nucleic Acids Res. 37:5343-5352(2009).
RN   [9]
RP   FUNCTION IN T(6)A37 FORMATION.
RX   PubMed=21183954; DOI=10.1038/emboj.2010.343;
RA   Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W.,
RA   Sternglanz R.;
RT   "The highly conserved KEOPS/EKC complex is essential for a universal tRNA
RT   modification, t6A.";
RL   EMBO J. 30:873-881(2011).
RN   [10]
RP   FUNCTION IN T(6)A37 FORMATION.
RX   PubMed=21285948; DOI=10.1038/emboj.2010.363;
RA   El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P.,
RA   Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.;
RT   "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA
RT   modification.";
RL   EMBO J. 30:882-893(2011).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-39; ASP-43; ASP-44; ILE-77;
RP   ARG-104; LYS-130; VAL-134; HIS-145; HIS-149; SER-172; ARG-207; SER-258 AND
RP   ASP-361.
RX   PubMed=23620299; DOI=10.1093/nar/gkt322;
RA   Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I.,
RA   Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C.,
RA   Caudy A.A., Durocher D., Sicheri F.;
RT   "Reconstitution and characterization of eukaryotic N6-
RT   threonylcarbamoylation of tRNA using a minimal enzyme system.";
RL   Nucleic Acids Res. 41:6332-6346(2013).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH AMP AND ZINC, AND SUBUNIT.
RX   PubMed=25084372; DOI=10.1107/s2053230x14014046;
RA   Tominaga T., Kobayashi K., Ishii R., Ishitani R., Nureki O.;
RT   "Structure of Saccharomyces cerevisiae mitochondrial Qri7 in complex with
RT   AMP.";
RL   Acta Crystallogr. F 70:1009-1014(2014).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC       codons beginning with adenine. Probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37. Involved in mitochondrial genome maintenance.
CC       {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:19578062,
CC       ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:21285948}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + AMP + H(+);
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03179,
CC         ECO:0000269|PubMed:23620299};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03179,
CC         ECO:0000269|PubMed:23620299, ECO:0000269|PubMed:25084372};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03179, ECO:0000269|PubMed:23620299,
CC       ECO:0000269|PubMed:25084372};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179,
CC       ECO:0000269|PubMed:23620299, ECO:0000269|PubMed:25084372}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961,
CC       ECO:0000269|PubMed:23620299}.
CC   -!- DISRUPTION PHENOTYPE: Loss of QRI7 leads to the formation of
CC       mitochondria with abnormal morphology and no DNA.
CC       {ECO:0000269|PubMed:19578062}.
CC   -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_03179}.
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DR   EMBL; X79380; CAA55926.1; -; Genomic_DNA.
DR   EMBL; X95644; CAA64909.1; -; Genomic_DNA.
DR   EMBL; Z74152; CAA98671.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11756.1; -; Genomic_DNA.
DR   PIR; S50740; S50740.
DR   RefSeq; NP_010179.1; NM_001180163.1.
DR   PDB; 3WUH; X-ray; 2.94 A; A/B=30-407.
DR   PDB; 4K25; X-ray; 2.88 A; A=30-407.
DR   PDB; 6NBJ; X-ray; 2.94 A; A/B=30-407.
DR   AlphaFoldDB; P43122; -.
DR   SMR; P43122; -.
DR   BioGRID; 31958; 187.
DR   DIP; DIP-5028N; -.
DR   FunCoup; P43122; 513.
DR   IntAct; P43122; 1.
DR   STRING; 4932.YDL104C; -.
DR   PaxDb; 4932-YDL104C; -.
DR   PeptideAtlas; P43122; -.
DR   EnsemblFungi; YDL104C_mRNA; YDL104C; YDL104C.
DR   GeneID; 851454; -.
DR   KEGG; sce:YDL104C; -.
DR   AGR; SGD:S000002262; -.
DR   SGD; S000002262; QRI7.
DR   VEuPathDB; FungiDB:YDL104C; -.
DR   eggNOG; KOG2707; Eukaryota.
DR   HOGENOM; CLU_023208_4_1_1; -.
DR   InParanoid; P43122; -.
DR   OMA; AAAHEIY; -.
DR   OrthoDB; 10259622at2759; -.
DR   BioCyc; MetaCyc:YDL104C-MONOMER; -.
DR   BioCyc; YEAST:YDL104C-MONOMER; -.
DR   BRENDA; 2.3.1.234; 984.
DR   BioGRID-ORCS; 851454; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P43122; -.
DR   PRO; PR:P43122; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P43122; protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IMP:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; EXP:UniProtKB.
DR   GO; GO:0008252; F:nucleotidase activity; IDA:SGD.
DR   GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR   GO; GO:0061711; F:tRNA N(6)-L-threonylcarbamoyladenine synthase activity; IDA:SGD.
DR   GO; GO:0072670; P:mitochondrial tRNA threonylcarbamoyladenosine modification; IMP:SGD.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:SGD.
DR   CDD; cd24097; ASKHA_NBD_TsaD-like; 1.
DR   FunFam; 3.30.420.40:FF:000297; tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial; 1.
DR   FunFam; 3.30.420.40:FF:000354; tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR022450; TsaD.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Metal-binding; Mitochondrion;
KW   Reference proteome; Transferase; Transit peptide; tRNA processing.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT   CHAIN           31..407
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT                   /id="PRO_0000096988"
FT   BINDING         145
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:23620299"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:23620299"
FT   BINDING         170..174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         328..329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:25084372"
FT   BINDING         361
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT                   ECO:0000269|PubMed:23620299"
FT   MUTAGEN         39
FT                   /note="E->A: Severely impairs t(6)A37 formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         43
FT                   /note="D->A: Severely impairs t(6)A37 formation. No effect
FT                   on dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         44
FT                   /note="D->A: Severely impairs t(6)A37 formation. No effect
FT                   on dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         77
FT                   /note="I->E: Severely impairs t(6)A37 formation. No effect
FT                   on dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         104
FT                   /note="R->A: Reduces enzyme activity by 35%. Partially
FT                   impairs dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         130
FT                   /note="K->A: Severely impairs t(6)A37 formation. Partially
FT                   impairs dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         134
FT                   /note="V->R: Severely impairs t(6)A37 formation. Prevents
FT                   dimerization."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         145
FT                   /note="H->A: Severely impairs t(6)A37 formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         149
FT                   /note="H->A: Severely impairs t(6)A37 formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         172
FT                   /note="S->K: Severely impairs t(6)A37 formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         207
FT                   /note="R->A: Severely impairs t(6)A37 formation. No effect
FT                   on dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         258
FT                   /note="S->A: Severely impairs t(6)A37 formation. No effect
FT                   on dimer formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   MUTAGEN         361
FT                   /note="D->A: Severely impairs t(6)A37 formation."
FT                   /evidence="ECO:0000269|PubMed:23620299"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          41..51
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          60..67
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:6NBJ"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:6NBJ"
FT   HELIX           82..99
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           119..136
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   TURN            155..158
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:3WUH"
FT   STRAND          164..174
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          176..185
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          187..195
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           198..209
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           216..224
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:6NBJ"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           259..270
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           281..309
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   TURN            311..316
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          320..325
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           330..339
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:3WUH"
FT   HELIX           356..359
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           364..372
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   HELIX           373..377
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   TURN            394..398
FT                   /evidence="ECO:0007829|PDB:4K25"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:4K25"
SQ   SEQUENCE   407 AA;  45543 MW;  328A21F239D6DB25 CRC64;
     MISIKGTGRF LLDNYRIWQR RAFNRPIQLR KGYKVLAIET SCDDTCVSVL DRFSKSAAPN
     VLANLKDTLD SIDEGGIIPT KAHIHHQARI GPLTERALIE SNAREGIDLI CVTRGPGMPG
     SLSGGLDFAK GLAVAWNKPL IGVHHMLGHL LIPRMGTNGK VPQFPFVSLL VSGGHTTFVL
     SRAIDDHEIL CDTIDIAVGD SLDKCGRELG FKGTMIAREM EKFINQDIND QDFALKLEMP
     SPLKNSASKR NMLSFSFSAF ITALRTNLTK LGKTEIQELP EREIRSIAYQ VQESVFDHII
     NKLKHVLKSQ PEKFKNVREF VCSGGVSSNQ RLRTKLETEL GTLNSTSFFN FYYPPMDLCS
     DNSIMIGWAG IEIWESLRLV SDLDICPIRQ WPLNDLLSVD GWRTDQL
//