ID   COX17_DICDI             Reviewed;          60 AA.
AC   Q54ID0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cytochrome c oxidase copper chaperone;
GN   Name=cox17; ORFNames=DDB_G0288831;
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: Copper chaperone for cytochrome c oxidase (COX). Binds two
CC       copper ions and deliver them to the Cu(A) site of COX (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COX17 family. {ECO:0000305}.
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DR   EMBL; AAFI02000125; EAL63037.1; -; Genomic_DNA.
DR   RefSeq; XP_636547.1; XM_631455.1.
DR   AlphaFoldDB; Q54ID0; -.
DR   SMR; Q54ID0; -.
DR   STRING; 44689.DDB0305161; -.
DR   PaxDb; Q54ID0; -.
DR   EnsemblProtists; EAL63037; EAL63037; DDB_G0288831.
DR   GeneID; 8626832; -.
DR   KEGG; ddi:DDB_G0288831; -.
DR   dictyBase; DDB_G0288831; cox17.
DR   eggNOG; KOG3496; Eukaryota.
DR   HOGENOM; CLU_149618_1_1_1; -.
DR   InParanoid; Q54ID0; -.
DR   OMA; KPLKACC; -.
DR   PhylomeDB; Q54ID0; -.
DR   PRO; PR:Q54ID0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0016531; F:copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR   InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR   InterPro; IPR007745; Cyt_c_oxidase_Cu-chaperone.
DR   PANTHER; PTHR16719; PTHR16719; 1.
DR   Pfam; PF05051; COX17; 1.
DR   SUPFAM; SSF47072; SSF47072; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Disulfide bond; Metal-binding; Mitochondrion;
KW   Reference proteome.
FT   CHAIN           1..60
FT                   /note="Cytochrome c oxidase copper chaperone"
FT                   /id="PRO_0000327790"
FT   DOMAIN          20..60
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           23..33
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           42..52
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   BINDING         20
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   BINDING         21
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   DISULFID        23..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        33..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   60 AA;  6586 MW;  7B9F3DF397334A8D CRC64;
     MSIAETNTTT EVAAPKKKMC CACPETKKVR DECIVANGEE KCAALIELHK VCLRKEGFDV