(data stored in ACNUC9543 zone)

SWISSPROT: DRE2_PLAF7

ID   DRE2_PLAF7              Reviewed;         266 AA.
AC   C0H4X5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
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=MAL8P1.31;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7;
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C.,
RA   Chillingworth T., Christodoulou Z., Clark L., Clark R., Corton C.,
RA   Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J.,
RA   Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z.,
RA   Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P.,
RA   Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A.,
RA   Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N.,
RA   Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L.,
RA   Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E.,
RA   Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M.,
RA   Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K.,
RA   Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T.,
RA   James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A.,
RA   Kyes S., Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J.,
RA   Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W.,
RA   Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S.,
RA   Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M.,
RA   Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C.,
RA   Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Nature 419:498-511(2002).
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
CC       chain functioning in an early step of cytosolic Fe-S biogenesis,
CC       facilitating the de novo assembly of a [4Fe-4S] cluster on the
CC       cytosolic Fe-S scaffold complex. Electrons are transferred from
CC       NADPH via a FAD- and FMN-containing diflavin oxidoreductase.
CC       Together with the diflavin oxidoreductase, also required for the
CC       assembly of the diferric tyrosyl radical cofactor of
CC       ribonucleotide reductase (RNR), probably by providing electrons
CC       for reduction during radical cofactor maturation in the catalytic
CC       small subunit. {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-
CC       Rule:MF_03115}.
CC   -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is
CC       otherwise mostly in an intrinsically disordered conformation.
CC       {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC       adenosyl-L-methionine-dependent methyltransferases, but does not
CC       bind S-adenosyl-L-methionine. It is required for correct assembly
CC       of the 2 Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by
CC       the mitochondrial MIA40-ERV1 disulfide relay system. The formation
CC       of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide
CC       exchange reactions effectively traps the protein in the
CC       mitochondrial intermembrane space. {ECO:0000255|HAMAP-
CC       Rule:MF_03115}.
CC   -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC       Rule:MF_03115}.
DR   EMBL; AL844507; CAX64153.1; -; Genomic_DNA.
DR   RefSeq; XP_002808875.1; XM_002808829.1.
DR   SMR; C0H4X5; -.
DR   SwissPalm; C0H4X5; -.
DR   PRIDE; C0H4X5; -.
DR   EnsemblProtists; CAX64153; CAX64153; PF3D7_0824600.
DR   GeneDB; PF3D7_0824600.1:pep; -.
DR   GeneID; 2655414; -.
DR   KEGG; pfa:PF3D7_0824600; -.
DR   EuPathDB; PlasmoDB:PF3D7_0824600; -.
DR   HOGENOM; HOG000282613; -.
DR   InParanoid; C0H4X5; -.
DR   KO; K22746; -.
DR   OMA; KECLYNG; -.
DR   Proteomes; UP000001450; Chromosome 8.
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   PANTHER; PTHR13273; PTHR13273; 1.
DR   Pfam; PF05093; CIAPIN1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0H4X5.
DR   SWISS-2DPAGE; C0H4X5.
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; Reference proteome.
FT   CHAIN         1    266       Anamorsin homolog.
FT                                /FTId=PRO_0000392356.
FT   REGION        1    164       N-terminal SAM-like domain.
FT                                {ECO:0000255|HAMAP-Rule:MF_03115}.
FT   REGION      165    185       Linker. {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   REGION      186    266       Intrinsically disordered.
FT                                {ECO:0000255|HAMAP-Rule:MF_03115}.
FT   REGION      229    243       Fe-S binding site B. {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   MOTIF       229    232       Cx2C motif 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   MOTIF       240    243       Cx2C motif 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   METAL       229    229       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   METAL       232    232       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   METAL       240    240       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
FT   METAL       243    243       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_03115}.
SQ   SEQUENCE   266 AA;  30838 MW;  A9AB964074592C14 CRC64;
     MIINFVGNTL IIFNEDIPCD LLRKKYKELF VPTISVLDFK KKRLYRKYNN IFLYTYKNYS
     FLWELENNIL HKVQKCLNKN GILKLIIYLN KNDVITPDKH ENKNNNDIKV NIDQKDYCEN
     YINDIFKNIK KECLYNGFIN IVNETSVAEN GIILNITAEN PDFLSNEDND VSSDDEDLYN
     NEDDKKKVVN RVCDNCTCGK KEKLLNSENK VLINEKDGEY ITENVVSSCG NCYLGDAFRC
     ASCPYKGLPA FQPGENVKLN LNNESN
//

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