DRE2_SCHMA
ID DRE2_SCHMA Reviewed; 272 AA.
AC C4PYP8; G4VQR6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 61.
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=Smp_207000;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=19606141; DOI=10.1038/nature08160;
RA Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P.,
RA Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D.,
RA Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A.,
RA Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T.,
RA Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y.,
RA Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P.,
RA Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J.,
RA Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M.,
RA Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J.,
RA Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G.,
RA El-Sayed N.M.;
RT "The genome of the blood fluke Schistosoma mansoni.";
RL Nature 460:352-358(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(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. 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; HE601631; CCD81528.1; -; Genomic_DNA.
DR RefSeq; XP_018654124.1; XM_018788597.1.
DR AlphaFoldDB; C4PYP8; -.
DR STRING; 6183.Smp_207000.1; -.
DR EnsemblMetazoa; Smp_207000.1; Smp_207000.1; Smp_207000.
DR GeneID; 29830877; -.
DR KEGG; smm:Smp_207000; -.
DR WBParaSite; Smp_207000.1; Smp_207000.1; Smp_207000.
DR CTD; 29830877; -.
DR eggNOG; KOG4020; Eukaryota.
DR HOGENOM; CLU_064393_1_0_1; -.
DR InParanoid; C4PYP8; -.
DR OrthoDB; 1588798at2759; -.
DR PhylomeDB; C4PYP8; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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..272
FT /note="Anamorsin homolog"
FT /id="PRO_0000392331"
FT REGION 1..151
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 151..185
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 192..213
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 233..247
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 233..236
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 244..247
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 192
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 208
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 211
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 213
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ SEQUENCE 272 AA; 29662 MW; 11A38702F71B84D8 CRC64;
MEQCVADCLN SDDCVMIVWS GEVQEDVMRG LQVAVSTYVK KLQFENLEKF VDSSAVDSQL
HECSVILCGW PNSISVNILK LGLLSNLLSC LRPGGRFFGR DLITGDWDSL KKNLTLSGYI
NPYQLSCENH LIFSASVPSN YTQGSSVKLP WANSDVEAAW ENVDNSSDAN GNIINTNTLL
QKSDLKTPLS VCGKEAATDS VGKKKRACKN CTCGLAEIEA AEEDKSDVPI SSCGNCYLGD
AFRCSTCPYR GLPPFKPGER ILIPDDVLRA DL
