DRE2_YEAST
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 03-AUG-2022, entry version 169.
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}; 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=3; 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 (ECO:0000255|HAMAP-Rule:MF_03115,
CC PubMed:27166425). {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}.
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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; 37.
DR ComplexPortal; CPX-386; TAH18-DRE2 complex.
DR DIP; DIP-6716N; -.
DR IntAct; P36152; 5.
DR MINT; P36152; -.
DR STRING; 4932.YKR071C; -.
DR iPTMnet; P36152; -.
DR MaxQB; P36152; -.
DR PaxDb; P36152; -.
DR PRIDE; P36152; -.
DR EnsemblFungi; YKR071C_mRNA; YKR071C; YKR071C.
DR GeneID; 853945; -.
DR KEGG; sce:YKR071C; -.
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 BioCyc; YEAST:G3O-32037-MON; -.
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: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 GO; GO:1905118; P:positive regulation of ribonucleoside-diphosphate reductase activity; IMP:ComplexPortal.
DR DisProt; DP01320; -.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR031838; Dre2_N.
DR PANTHER; PTHR13273; PTHR13273; 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
