DRE22_PARTE
ID DRE22_PARTE Reviewed; 250 AA.
AC A0CIS3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Anamorsin homolog 2 {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03115};
GN ORFNames=GSPATT00007825001;
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; CT868085; CAK70690.1; -; Genomic_DNA.
DR RefSeq; XP_001438087.1; XM_001438050.1.
DR AlphaFoldDB; A0CIS3; -.
DR SMR; A0CIS3; -.
DR STRING; 5888.CAK70690; -.
DR EnsemblProtists; CAK70690; CAK70690; GSPATT00007825001.
DR GeneID; 5023872; -.
DR KEGG; ptm:GSPATT00007825001; -.
DR eggNOG; KOG4020; Eukaryota.
DR HOGENOM; CLU_929001_0_0_1; -.
DR InParanoid; A0CIS3; -.
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 2"
FT /id="PRO_0000392354"
FT REGION 1..102
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 102..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; 28605 MW; 73BA130E7F79A3FB CRC64;
MNLKITINQQ ASISEKLIIA NLEQLLIFRD NTFNKIDCDQ QITLKDAVQI SQILNDQGVL
NYEGEINEQI TTYLEACGLY SQGQGQFIKR TLQTKKINIP QQDFNNCYGK YDYIEQKFQN
QINFFKQVDL KGNQETIDEN ELLNDGVEVK QVESCASKPR ACANCTCGRK EMEEKQDKEQ
LLEQLKNNSV KGCGSCYLGD AFRCANCPFR GLPAFKDGEQ VKVLQDDVFL KEKEETDQIK
LENGKVKLMI
