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DRE2_CAEEL
ID   DRE2_CAEEL              Reviewed;         238 AA.
AC   P41847;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Anamorsin homolog {ECO:0000255|HAMAP-Rule:MF_03115};
DE   AltName: Full=Fe-S cluster assembly protein DRE2 homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN   ORFNames=T20B12.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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. Part of an electron transfer chain
CC       functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC       the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S
CC       scaffold complex. Electrons are transferred from NADPH via a FAD- and
CC       FMN-containing diflavin oxidoreductase. Together with the diflavin
CC       oxidoreductase, 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. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}.
CC       Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}.
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}.
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. It is required for correct assembly of the 2
CC       Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115}.
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   -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC       Rule:MF_03115}.
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DR   EMBL; FO081094; CCD69077.1; -; Genomic_DNA.
DR   PIR; T16907; T16907.
DR   RefSeq; NP_498632.1; NM_066231.3.
DR   AlphaFoldDB; P41847; -.
DR   BioGRID; 41260; 7.
DR   DIP; DIP-25608N; -.
DR   IntAct; P41847; 1.
DR   STRING; 6239.T20B12.7; -.
DR   EPD; P41847; -.
DR   PaxDb; P41847; -.
DR   PeptideAtlas; P41847; -.
DR   EnsemblMetazoa; T20B12.7.1; T20B12.7.1; WBGene00020604.
DR   GeneID; 176051; -.
DR   KEGG; cel:CELE_T20B12.7; -.
DR   UCSC; T20B12.7.1; c. elegans.
DR   CTD; 176051; -.
DR   WormBase; T20B12.7; CE01413; WBGene00020604; -.
DR   eggNOG; KOG4020; Eukaryota.
DR   GeneTree; ENSGT00390000011417; -.
DR   HOGENOM; CLU_064393_3_0_1; -.
DR   InParanoid; P41847; -.
DR   OMA; AEVCNTV; -.
DR   OrthoDB; 1449635at2759; -.
DR   PhylomeDB; P41847; -.
DR   PRO; PR:P41847; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00020604; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   HAMAP; MF_03115; Anamorsin; 1.
DR   InterPro; IPR007785; Anamorsin.
DR   InterPro; IPR046408; CIAPIN1.
DR   PANTHER; PTHR13273; PTHR13273; 1.
DR   Pfam; PF05093; CIAPIN1; 2.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome.
FT   CHAIN           1..238
FT                   /note="Anamorsin homolog"
FT                   /id="PRO_0000065475"
FT   REGION          1..121
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          121..150
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          163..180
FT                   /note="Fe-S binding site A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          202..216
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           202..205
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           213..216
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         163
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         175
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         178
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         180
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         213
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         216
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ   SEQUENCE   238 AA;  25551 MW;  932AC911ECC3EEB0 CRC64;
     MSILSDFLKH PNLLQVTDGG PLVDGTNGVK GTRVVGSVSN ARELRGADSL VGDVERAIIQ
     VQETELLAEV CNTVFDVMKQ NGEVIVFSQD LTTAQRKLRI AGFRVTEVAA EFPVRGIKLV
     NFGEKVALDL GVVADEDLID EDGLLQEEDF EKPTGDQLKA GGCGPDDPNK KKRACKNCSC
     GLAEQEELEK MGQIAAEPKS SCGNCSLGDA FRCSTCPYLG QPPFKPGETV KISTVDDF
 
 
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