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COX17_SCHPO
ID   COX17_SCHPO             Reviewed;          70 AA.
AC   Q9P7Z7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Cytochrome c oxidase copper chaperone;
GN   Name=cox17; ORFNames=SPBC26H8.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329671; CAB75401.1; -; Genomic_DNA.
DR   RefSeq; NP_596649.1; NM_001022571.2.
DR   AlphaFoldDB; Q9P7Z7; -.
DR   SMR; Q9P7Z7; -.
DR   STRING; 4896.SPBC26H8.14c.1; -.
DR   MaxQB; Q9P7Z7; -.
DR   PaxDb; Q9P7Z7; -.
DR   EnsemblFungi; SPBC26H8.14c.1; SPBC26H8.14c.1:pep; SPBC26H8.14c.
DR   GeneID; 2540423; -.
DR   KEGG; spo:SPBC26H8.14c; -.
DR   PomBase; SPBC26H8.14c; cox17.
DR   VEuPathDB; FungiDB:SPBC26H8.14c; -.
DR   eggNOG; KOG3496; Eukaryota.
DR   HOGENOM; CLU_149618_1_3_1; -.
DR   InParanoid; Q9P7Z7; -.
DR   OMA; QYKTCMA; -.
DR   PhylomeDB; Q9P7Z7; -.
DR   PRO; PR:Q9P7Z7; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; ISS:PomBase.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:PomBase.
DR   GO; GO:0016531; F:copper chaperone activity; ISS:PomBase.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:PomBase.
DR   GO; GO:0015680; P:protein maturation by copper ion transfer; ISS:PomBase.
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..70
FT                   /note="Cytochrome c oxidase copper chaperone"
FT                   /id="PRO_0000239059"
FT   DOMAIN          28..70
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           31..41
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           52..62
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   BINDING         29
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   DISULFID        31..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        41..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   70 AA;  7493 MW;  B56C3AD2C763E9FB CRC64;
     MSSSTEPSTA TKVSEPAPIA SEEKPKPCCA CPETKQARDA CMLQSSNGPI ECAKLIEAHK
     KCMAQYGYEV
 
 
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