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DRE21_PARTE
ID   DRE21_PARTE             Reviewed;         250 AA.
AC   A0BV78;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Anamorsin homolog 1 {ECO:0000255|HAMAP-Rule:MF_03115};
DE   AltName: Full=Fe-S cluster assembly protein DRE2 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03115};
GN   ORFNames=GSPATT00005691001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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; CT868019; CAK62445.1; -; Genomic_DNA.
DR   RefSeq; XP_001429843.1; XM_001429806.1.
DR   AlphaFoldDB; A0BV78; -.
DR   SMR; A0BV78; -.
DR   STRING; 5888.CAK62445; -.
DR   EnsemblProtists; CAK62445; CAK62445; GSPATT00005691001.
DR   GeneID; 5015627; -.
DR   KEGG; ptm:GSPATT00005691001; -.
DR   eggNOG; KOG4020; Eukaryota.
DR   HOGENOM; CLU_929001_0_0_1; -.
DR   InParanoid; A0BV78; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
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; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome.
FT   CHAIN           1..250
FT                   /note="Anamorsin homolog 1"
FT                   /id="PRO_0000392353"
FT   REGION          1..104
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          104..149
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          155..167
FT                   /note="Fe-S binding site A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          193..207
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           193..196
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           204..207
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         155
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         162
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         165
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         167
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         204
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         207
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ   SEQUENCE   250 AA;  28631 MW;  B78FE03E4427138B CRC64;
     MNLKITINQQ ASISDSLIIA NLNLIQFFRD NTFNKIECDQ LLTLKDAVQI SQILKDQGVL
     IYEGEINESV ITYFQASGLY NQGQGKFIKQ VLQIKKLNIP QQEFNNCYGK YDYIEQKFQN
     QINFFKQVDI NGKQEIIDEN ELLDDGVQVK QVESCASKPR ACANCTCGRK EMEEKQDKEQ
     LLEQLKNNSI KGCGSCYLGD AFRCANCPYR GLPAFKDGEQ VKVLQDDVFL QEQEEKDQVK
     LENGKVKLKI
 
 
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