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ISCA2_DICDI
ID   ISCA2_DICDI             Reviewed;         209 AA.
AC   Q54P40;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Iron-sulfur cluster assembly 2 homolog, mitochondrial;
DE   AltName: Full=Iron-sulfur assembly protein isca2;
DE   Flags: Precursor;
GN   Name=isca2; ORFNames=DDB_G0284809;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC       functioning late in the iron-sulfur cluster assembly pathway. May be
CC       involved in the binding of an intermediate of Fe/S cluster assembly.
CC       {ECO:0000250|UniProtKB:Q86U28}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per dimer. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q86U28}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR   EMBL; AAFI02000071; EAL65057.1; -; Genomic_DNA.
DR   RefSeq; XP_638418.1; XM_633326.1.
DR   AlphaFoldDB; Q54P40; -.
DR   SMR; Q54P40; -.
DR   STRING; 44689.DDB0235144; -.
DR   PaxDb; Q54P40; -.
DR   EnsemblProtists; EAL65057; EAL65057; DDB_G0284809.
DR   GeneID; 8624788; -.
DR   KEGG; ddi:DDB_G0284809; -.
DR   dictyBase; DDB_G0284809; isca2.
DR   eggNOG; KOG1119; Eukaryota.
DR   HOGENOM; CLU_069054_1_0_1; -.
DR   InParanoid; Q54P40; -.
DR   OMA; MNESSLM; -.
DR   PhylomeDB; Q54P40; -.
DR   Reactome; R-DDI-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   PRO; PR:Q54P40; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IBA:GO_Central.
DR   Gene3D; 2.60.300.12; -; 1.
DR   InterPro; IPR000361; FeS_biogenesis.
DR   InterPro; IPR016092; FeS_cluster_insertion.
DR   InterPro; IPR035903; HesB-like_dom_sf.
DR   Pfam; PF01521; Fe-S_biosyn; 1.
DR   SUPFAM; SSF89360; SSF89360; 1.
DR   TIGRFAMs; TIGR00049; TIGR00049; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..209
FT                   /note="Iron-sulfur cluster assembly 2 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000393700"
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         199
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ   SEQUENCE   209 AA;  23712 MW;  8B65781740FCD6F3 CRC64;
     MIRSIFKKNS SLPYFLKRSF ITKPHSIITP IINNNNHNNN NINTPIKNIQ SFNFKFFTTT
     TTSNPIHQQT TTTTTTTPST EQQQLSKEAE EINENITKYN ITLTDSCVKE LNSVQKKSDS
     TDIFLRVMVD MGGCSGYQYI IKVENKLQDD DVLFIRNGAK VIIDKISLEM MEGSIIDYET
     ALMRSSFVVA SNPNTIKSCG CKISFELKK
 
 
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