(data stored in SCRATCH zone)

SWISSPROT: COX1_THEAN

ID   COX1_THEAN              Reviewed;         480 AA.
AC   Q4UJ69;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   11-DEC-2019, entry version 71.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=MT-CO1; Synonyms=COI, COXI, MTCO1; ORFNames=Tap370b08.q2ca38.01;
OS   Theileria annulata.
OG   Mitochondrion.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara;
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA   Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA   Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA   McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA   Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA   Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA   Shiels B., Tait A., Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata compared
RT   with T. parva.";
RL   Science 309:131-133(2005).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. CO I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme A of subunit
CC       1 to the bimetallic center formed by heme A3 and copper B (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC         + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC         COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1;
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI72674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR940346; CAI72674.1; ALT_INIT; Genomic_DNA.
DR   STRING; 5874.XP_954716.1; -.
DR   PRIDE; Q4UJ69; -.
DR   eggNOG; KOG4769; Eukaryota.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085274; -.
DR   InParanoid; Q4UJ69; -.
DR   OrthoDB; 728231at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001950; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4UJ69.
DR   SWISS-2DPAGE; Q4UJ69.
KW   Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..480
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000233106"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   METAL           69
FT                   /note="Iron (heme A axial ligand)"
FT                   /evidence="ECO:0000250"
FT   METAL           246
FT                   /note="Copper B"
FT                   /evidence="ECO:0000250"
FT   METAL           250
FT                   /note="Copper B"
FT                   /evidence="ECO:0000250"
FT   METAL           382
FT                   /note="Iron (heme A3 axial ligand)"
FT                   /evidence="ECO:0000250"
FT   METAL           384
FT                   /note="Iron (heme A axial ligand)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        246..250
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  53241 MW;  AE9889CE4FEB58AE CRC64;
     MVFEFVLSLF NSVSGNHKII GISYLWLAYW FGMIGFYMSV LIRTELGMSG LKIITMDTLE
     IYNLLFTLHG LIMVFFNIMT GLFGGIGNYL YPVLLGSCDV VYPRVNLYSL LLQPIGFVLV
     VSSVYLEIGS GTGWTLYPPL STSLSNIGID LIIFGLLAAG IASTLSSINF ITTFASIKTI
     GFVIDRISPA AWSIVLTSFL LLLSLPVVTA VFLMVFFDRN HSTMFFESSN SGDPILYQHL
     FWFFGHPEVY IMILPGFGII SLLLSTYTTK EMFGNQTMIL AMGSIALLGC LVWGHHMYTS
     GLEADTRGYF TTVTILIALP TGNKIFNWVT TLQCVESIKS LGLILFAVLF IVNFVIGGTT
     GVVLGNAGLD VVLHDTVYVV GHFHFVLSIG AIISLICFIV YIQRMLFGII LSNRLLSLMA
     PIFMIAVLFT FLPMHFTGFS PLPRRIPDYP DEMWGWNFIC TLGATMMLVL KLTVLFIISL
//

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