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Protein

Fe-S cluster assembly protein DRE2

Gene

DRE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2. Has anti-apoptotic effects in the cell. Involved in negative control of H2O2-induced cell death.UniRule annotation7 Publications

Miscellaneous

Present with 1050 molecules/cell in log phase SD medium.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi252Iron-sulfur (2Fe-2S)UniRule annotation1 Publication1
Metal bindingi263Iron-sulfur (2Fe-2S)UniRule annotation1 Publication1
Metal bindingi266Iron-sulfur (2Fe-2S)UniRule annotation1 Publication1
Metal bindingi268Iron-sulfur (2Fe-2S)UniRule annotation1 Publication1
Metal bindingi311Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi314Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi322Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi325Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • electron transfer activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • iron-sulfur cluster assembly Source: SGD
  • negative regulation of hydrogen peroxide-mediated programmed cell death Source: SGD
  • negative regulation of nitric oxide biosynthetic process Source: SGD

Keywordsi

Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32037-MONOMER
ReactomeiR-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)

Names & Taxonomyi

Protein namesi
Recommended name:
Fe-S cluster assembly protein DRE2UniRule annotation
Alternative name(s):
Anamorsin homologUniRule annotation
Gene namesi
Name:DRE2UniRule annotation
Ordered Locus Names:YKR071C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR071C
SGDiS000001779 DRE2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002032191 – 348Fe-S cluster assembly protein DRE2Add BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei206PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP36152
PaxDbiP36152
PRIDEiP36152

PTM databases

iPTMnetiP36152

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with TAH18. Interacts with MIA40.UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAH18Q121817EBI-26482,EBI-37624

Protein-protein interaction databases

BioGridi34202, 35 interactors
DIPiDIP-6716N
IntActiP36152, 10 interactors
MINTiP36152
STRINGi4932.YKR071C

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi13 – 16Combined sources4
Helixi19 – 31Combined sources13
Beta strandi34 – 41Combined sources8
Helixi42 – 47Combined sources6
Beta strandi54 – 56Combined sources3
Beta strandi59 – 63Combined sources5
Helixi75 – 82Combined sources8
Helixi96 – 105Combined sources10
Beta strandi107 – 110Combined sources4
Beta strandi112 – 114Combined sources3
Beta strandi116 – 119Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KM1NMR-A1-133[»]
ProteinModelPortaliP36152
SMRiP36152
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36152

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 158N-terminal SAM-like domainUniRule annotation1 PublicationAdd BLAST158
Regioni159 – 242LinkerUniRule annotationCuratedAdd BLAST84
Regioni243 – 348Intrinsically disorderedUniRule annotationCuratedAdd BLAST106
Regioni252 – 268Fe-S binding site AUniRule annotationCuratedAdd BLAST17
Regioni311 – 325Fe-S binding site BUniRule annotationCuratedAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi311 – 314Cx2C motif 1UniRule annotationCurated4
Motifi322 – 325Cx2C motif 2UniRule annotationCurated4

Domaini

The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine (PubMed:22487307). It is required for correct assembly of the 2 Fe-S clusters (ECO:0000255|HAMAP-Rule:MF_03115, PubMed:27166425).2 Publications
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.UniRule annotation1 Publication
The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the anamorsin family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000011417
HOGENOMiHOG000209024
InParanoidiP36152
OMAiGKKVGGC
OrthoDBiEOG092C54XZ

Family and domain databases

HAMAPiMF_03115 Anamorsin, 1 hit
InterProiView protein in InterPro
IPR007785 Anamorsin
IPR031838 Dre2_N
PANTHERiPTHR13273 PTHR13273, 1 hit
PfamiView protein in Pfam
PF05093 CIAPIN1, 1 hit
PF16803 DRE2_N, 1 hit

Sequencei

Sequence statusi: Complete.

P36152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQYKTGLLL IHPAVTTTPE LVENTKAQAA SKKVKFVDQF LINKLNDGSI
60 70 80 90 100
TLENAKYETV HYLTPEAQTD IKFPKKLISV LADSLKPNGS LIGLSDIYKV
110 120 130 140 150
DALINGFEII NEPDYCWIKM DSSKLNQTVS IPLKKKKTNN TKLQSGSKLP
160 170 180 190 200
TFKKASSSTS NLPSFKKADH SRQPIVKETD SFKPPSFKMT TEPKVYRVVD
210 220 230 240 250
DLIEDSDDDD FSSDSSKAQY FDQVDTSDDS IEEEELIDED GSGKSMITMI
260 270 280 290 300
TCGKSKTKKK KACKDCTCGM KEQEENEIND IRSQQDKVVK FTEDELTEID
310 320 330 340
FTIDGKKVGG CGSCSLGDAF RCSGCPYLGL PAFKPGQPIN LDSISDDL
Length:348
Mass (Da):38,543
Last modified:June 1, 1994 - v1
Checksum:i8F60A2D097839FB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28296 Genomic DNA Translation: CAA82150.1
BK006944 Genomic DNA Translation: DAA09222.1
PIRiS38148
RefSeqiNP_012997.3, NM_001179861.3

Genome annotation databases

EnsemblFungiiYKR071C; YKR071C; YKR071C
GeneIDi853945
KEGGisce:YKR071C

Similar proteinsi

Entry informationi

Entry nameiDRE2_YEAST
AccessioniPrimary (citable) accession number: P36152
Secondary accession number(s): D6VXD2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 25, 2018
This is version 143 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health