ID DRE2_YEAST Reviewed; 348 AA. AC P36152; D6VXD2; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Fe-S cluster assembly protein DRE2 {ECO:0000255|HAMAP-Rule:MF_03115}; DE AltName: Full=Anamorsin homolog {ECO:0000255|HAMAP-Rule:MF_03115}; GN Name=DRE2 {ECO:0000255|HAMAP-Rule:MF_03115}; GN OrderedLocusNames=YKR071C; 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=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). 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 FUNCTION. RX PubMed=12759774; DOI=10.1007/s00294-003-0407-2; RA Chanet R., Heude M.; RT "Characterization of mutations that are synthetic lethal with pol3-13, a RT mutated allele of DNA polymerase delta in Saccharomyces cerevisiae."; RL Curr. Genet. 43:337-350(2003). RN [4] 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 [5] 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 [6] RP UBIQUITINATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16432255; DOI=10.1074/mcp.m500368-mcp200; RA Tagwerker C., Flick K., Cui M., Guerrero C., Dou Y., Auer B., Baldi P., RA Huang L., Kaiser P.; RT "A tandem affinity tag for two-step purification under fully denaturing RT conditions: application in ubiquitin profiling and protein complex RT identification combined with in vivocross-linking."; RL Mol. Cell. Proteomics 5:737-748(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND DISRUPTION PHENOTYPE. RX PubMed=18625724; DOI=10.1128/mcb.00642-08; RA Zhang Y., Lyver E.R., Nakamaru-Ogiso E., Yoon H., Amutha B., Lee D.W., RA Bi E., Ohnishi T., Daldal F., Pain D., Dancis A.; RT "Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic RT Fe/S protein biogenesis."; RL Mol. Cell. Biol. 28:5569-5582(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY RP 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 [10] RP FUNCTION IN APOPTOSIS, AND INTERACTION WITH TAH18. RX PubMed=19194512; DOI=10.1371/journal.pone.0004376; RA Vernis L., Facca C., Delagoutte E., Soler N., Chanet R., Guiard B., RA Faye G., Baldacci G.; RT "A newly identified essential complex, Dre2-Tah18, controls mitochondria RT integrity and cell death after oxidative stress in yeast."; RL PLoS ONE 4:E4376-E4376(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP FUNCTION, AND COFACTOR. RX PubMed=20802492; DOI=10.1038/nchembio.432; RA Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.; RT "Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein RT biogenesis."; RL Nat. Chem. Biol. 6:758-765(2010). RN [13] RP SUBCELLULAR LOCATION, AND INTERACTION WITH MIA40. RX PubMed=21700214; DOI=10.1016/j.chembiol.2011.03.015; RA Banci L., Bertini I., Ciofi-Baffoni S., Boscaro F., Chatzi A., RA Mikolajczyk M., Tokatlidis K., Winkelmann J.; RT "Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40- RT dependent mitochondrial protein trapping machinery."; RL Chem. Biol. 18:794-804(2011). RN [14] RP FUNCTION. RX PubMed=21931161; DOI=10.1074/jbc.m111.294074; RA Zhang Y., Liu L., Wu X., An X., Stubbe J., Huang M.; RT "Investigation of in vivo diferric tyrosyl radical formation in RT Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution RT of Grx3/4 and Dre2 proteins."; RL J. Biol. Chem. 286:41499-41509(2011). RN [15] RP FUNCTION, AND INTERACTION WITH TAH18. RX PubMed=21902732; DOI=10.1111/j.1365-2958.2011.07788.x; RA Soler N., Delagoutte E., Miron S., Facca C., Baille D., d'Autreaux B., RA Craescu G., Frapart Y.M., Mansuy D., Baldacci G., Huang M.E., Vernis L.; RT "Interaction between the reductase Tah18 and highly conserved Fe-S RT containing Dre2 C-terminus is essential for yeast viability."; RL Mol. Microbiol. 82:54-67(2011). RN [16] RP FUNCTION. RX PubMed=24733891; DOI=10.1073/pnas.1405204111; RA Zhang Y., Li H., Zhang C., An X., Liu L., Stubbe J., Huang M.; RT "Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide RT reductase metallocofactor assembly and DNA synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E1695-E1704(2014). RN [17] RP COFACTOR. RX PubMed=27166425; DOI=10.1042/bcj20160416; RA Netz D.J., Genau H.M., Weiler B.D., Bill E., Pierik A.J., Lill R.; RT "The conserved protein Dre2 uses essential [2Fe-2S] and [4Fe-4S] clusters RT for its function in cytosolic iron-sulfur protein assembly."; RL Biochem. J. 473:2073-2085(2016). RN [18] RP COFACTOR. RX PubMed=27672211; DOI=10.1093/jb/mvw054; RA Zhang Y., Yang C., Dancis A., Nakamaru-Ogiso E.; RT "EPR studies of wild type and mutant Dre2 identify essential [2Fe--2S] and RT [4Fe--4S] clusters and their cysteine ligands."; RL J. Biochem. 161:67-78(2017). RN [19] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=31040179; DOI=10.1074/jbc.ra119.008600; RA Pandey A.K., Pain J., Dancis A., Pain D.; RT "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm RT for iron-sulfur cluster assembly and tRNA thiolation in yeast."; RL J. Biol. Chem. 294:9489-9502(2019). RN [20] RP STRUCTURE BY NMR OF 1-133, DOMAIN, AND COFACTOR. RX PubMed=22487307; DOI=10.1111/j.1742-4658.2012.08597.x; RA Soler N., Craescu C.T., Gallay J., Frapart Y.M., Mansuy D., Raynal B., RA Baldacci G., Pastore A., Huang M.E., Vernis L.; RT "A S-adenosylmethionine methyltransferase-like domain within the essential, RT Fe-S-containing yeast protein Dre2."; RL FEBS J. 279:2108-2119(2012). CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein CC assembly (CIA) machinery required for the maturation of CC extramitochondrial Fe-S proteins (PubMed:18625724, PubMed:19194512, CC PubMed:20802492, PubMed:21902732, PubMed:31040179). Part of an electron CC transfer chain functioning in an early step of cytosolic Fe-S CC biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on CC the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from CC NADPH via the FAD- and FMN-containing protein TAH18 (PubMed:20802492). CC TAH18-DRE2 are also required for the assembly of the diferric tyrosyl CC radical cofactor of ribonucleotide reductase (RNR), probably by CC providing electrons for reduction during radical cofactor maturation in CC the catalytic small subunit RNR2 (PubMed:21931161, PubMed:24733891). CC Has anti-apoptotic effects in the cell. Involved in negative control of CC H(2)O(2)-induced cell death (PubMed:19194512). {ECO:0000255|HAMAP- CC Rule:MF_03115, ECO:0000269|PubMed:12759774, CC ECO:0000269|PubMed:18625724, ECO:0000269|PubMed:19194512, CC ECO:0000269|PubMed:20802492, ECO:0000269|PubMed:21902732, CC ECO:0000269|PubMed:21931161, ECO:0000269|PubMed:24733891, CC ECO:0000269|PubMed:31040179}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115, CC ECO:0000269|PubMed:18625724, ECO:0000269|PubMed:20802492, CC ECO:0000269|PubMed:22487307}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115, CC ECO:0000269|PubMed:27166425, ECO:0000269|PubMed:27672211}; CC Note=In the presence of oxygen, the A site-bound [2Fe-2S] cluster is CC labile and the B site-bound [4Fe-4S] cluster is readily converted into CC a [2Fe-2S] cluster, a reason why recombinant protein is often isolated CC with a single [2Fe-2S] cluster. {ECO:0000305|PubMed:27166425, CC ECO:0000305|PubMed:27672211}; CC -!- SUBUNIT: Monomer (By similarity). Interacts with TAH18 CC (PubMed:19194512, PubMed:21902732). Interacts with MIA40 CC (PubMed:21700214). {ECO:0000250|UniProtKB:Q6FI81, ECO:0000255|HAMAP- CC Rule:MF_03115, ECO:0000269|PubMed:19194512, CC ECO:0000269|PubMed:21700214, ECO:0000269|PubMed:21902732}. CC -!- INTERACTION: CC P36152; Q12181: TAH18; NbExp=4; IntAct=EBI-26482, EBI-37624; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115, CC ECO:0000269|PubMed:18625724, ECO:0000269|PubMed:21700214}. CC Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115, CC ECO:0000269|PubMed:18625724, ECO:0000269|PubMed:21700214}. CC -!- DOMAIN: The N-terminal domain has structural similarity with S- CC adenosyl-L-methionine-dependent methyltransferases, but does not bind CC S-adenosyl-L-methionine (PubMed:22487307). It is required for correct CC assembly of the 2 Fe-S clusters (PubMed:27166425). {ECO:0000255|HAMAP- CC Rule:MF_03115, ECO:0000269|PubMed:22487307, CC ECO:0000269|PubMed:27166425}. CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise CC mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP- CC Rule:MF_03115, ECO:0000269|PubMed:22487307}. CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the CC mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 CC disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange CC reactions effectively traps the protein in the mitochondrial CC intermembrane space. {ECO:0000255|HAMAP-Rule:MF_03115, CC ECO:0000269|PubMed:21700214}. CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16432255}. CC -!- DISRUPTION PHENOTYPE: Inviable (PubMed:18625724). Decreases cytosolic CC iron-sulfur (Fe-S) protein assembly (PubMed:31040179). CC {ECO:0000269|PubMed:18625724, ECO:0000269|PubMed:31040179}. CC -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP- CC Rule:MF_03115}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z28296; CAA82150.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09222.1; -; Genomic_DNA. DR PIR; S38148; S38148. DR RefSeq; NP_012997.3; NM_001179861.3. DR PDB; 2KM1; NMR; -; A=1-133. DR PDBsum; 2KM1; -. DR AlphaFoldDB; P36152; -. DR BMRB; P36152; -. DR SMR; P36152; -. DR BioGRID; 34202; 42. DR ComplexPortal; CPX-386; TAH18-DRE2 complex. DR DIP; DIP-6716N; -. DR IntAct; P36152; 7. DR MINT; P36152; -. DR STRING; 4932.YKR071C; -. DR iPTMnet; P36152; -. DR MaxQB; P36152; -. DR PaxDb; 4932-YKR071C; -. DR PeptideAtlas; P36152; -. DR EnsemblFungi; YKR071C_mRNA; YKR071C; YKR071C. DR GeneID; 853945; -. DR KEGG; sce:YKR071C; -. DR AGR; SGD:S000001779; -. DR SGD; S000001779; DRE2. DR VEuPathDB; FungiDB:YKR071C; -. DR eggNOG; KOG4020; Eukaryota. DR GeneTree; ENSGT00390000011417; -. DR HOGENOM; CLU_067152_0_0_1; -. DR InParanoid; P36152; -. DR OMA; TMITCGK; -. DR OrthoDB; 52119at2759; -. DR BioCyc; YEAST:G3O-32037-MONOMER; -. DR BioGRID-ORCS; 853945; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P36152; -. DR PRO; PR:P36152; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36152; Protein. DR GO; GO:0097361; C:CIA complex; IDA:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; IMP:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:ComplexPortal. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:ComplexPortal. DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IMP:SGD. DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:SGD. DR DisProt; DP01320; -. DR Gene3D; 3.40.50.11000; Fe-S cluster assembly protein Dre2, N-terminal domain; 1. DR HAMAP; MF_03115; Anamorsin; 1. DR InterPro; IPR007785; Anamorsin. DR InterPro; IPR046408; CIAPIN1. DR InterPro; IPR031838; Dre2_N. DR PANTHER; PTHR13273; ANAMORSIN; 1. DR PANTHER; PTHR13273:SF14; ANAMORSIN; 1. DR Pfam; PF05093; CIAPIN1; 1. DR Pfam; PF16803; DRE2_N; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; KW Mitochondrion; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..348 FT /note="Fe-S cluster assembly protein DRE2" FT /id="PRO_0000203219" FT REGION 1..158 FT /note="N-terminal SAM-like domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000305|PubMed:22487307" FT REGION 137..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..242 FT /note="Linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000305" FT REGION 252..268 FT /note="Fe-S binding site A" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000305" FT REGION 311..325 FT /note="Fe-S binding site B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000305" FT MOTIF 311..314 FT /note="Cx2C motif 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000305" FT MOTIF 322..325 FT /note="Cx2C motif 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000305" FT COMPBIAS 137..167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 252 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 263 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 266 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 268 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 311 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 314 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 322 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT BINDING 325 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115, FT ECO:0000269|PubMed:27672211" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT STRAND 5..11 FT /evidence="ECO:0007829|PDB:2KM1" FT HELIX 13..16 FT /evidence="ECO:0007829|PDB:2KM1" FT HELIX 19..31 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:2KM1" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 59..63 FT /evidence="ECO:0007829|PDB:2KM1" FT HELIX 75..82 FT /evidence="ECO:0007829|PDB:2KM1" FT HELIX 96..105 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:2KM1" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:2KM1" SQ SEQUENCE 348 AA; 38543 MW; 8F60A2D097839FB3 CRC64; MSQYKTGLLL IHPAVTTTPE LVENTKAQAA SKKVKFVDQF LINKLNDGSI TLENAKYETV HYLTPEAQTD IKFPKKLISV LADSLKPNGS LIGLSDIYKV DALINGFEII NEPDYCWIKM DSSKLNQTVS IPLKKKKTNN TKLQSGSKLP TFKKASSSTS NLPSFKKADH SRQPIVKETD SFKPPSFKMT TEPKVYRVVD DLIEDSDDDD FSSDSSKAQY FDQVDTSDDS IEEEELIDED GSGKSMITMI TCGKSKTKKK KACKDCTCGM KEQEENEIND IRSQQDKVVK FTEDELTEID FTIDGKKVGG CGSCSLGDAF RCSGCPYLGL PAFKPGQPIN LDSISDDL //