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Database: UniProt
Entry: J4D689_THEOR
LinkDB: J4D689_THEOR
Original site: J4D689_THEOR 
ID   J4D689_THEOR            Unreviewed;       210 AA.
AC   J4D689;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=ATP synthase subunit delta {ECO:0000313|EMBL:BAM39420.1};
GN   ORFNames=TOT_010001314 {ECO:0000313|EMBL:BAM39420.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39420.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM39420.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM39420.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with differing
RT   abilities to transform leukocytes reveals key mediators of Theileria-
RT   induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000256|ARBA:ARBA00007046}.
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DR   EMBL; AP011946; BAM39420.1; -; Genomic_DNA.
DR   RefSeq; XP_009689721.1; XM_009691426.1.
DR   AlphaFoldDB; J4D689; -.
DR   STRING; 869250.J4D689; -.
DR   EnsemblProtists; BAM39420; BAM39420; TOT_010001314.
DR   GeneID; 20714113; -.
DR   KEGG; tot:TOT_010001314; -.
DR   VEuPathDB; PiroplasmaDB:TOT_010001314; -.
DR   eggNOG; KOG1662; Eukaryota.
DR   OrthoDB; 276144at2759; -.
DR   Proteomes; UP000003786; Chromosome 1.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR   PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR   PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ   SEQUENCE   210 AA;  23621 MW;  5CB17388417375CA CRC64;
     MYFKNVNSSY RLNFSTKKTE TPKLLDGFGI MGSYANALFL STQTVGNLNQ VMSDLKFVAD
     SLQSCEDFRT FMTTPGLRTS EKMKFLREDL GTLTGAPLQN QTLNCLEMLF EQKRSNEILN
     LAKHFETLFL SANNQLKCLV QSADPLNKDI KERIQEALKQ RLGGSYEPVV EYKVNPSLLG
     GLLVNVGDKV VDCSVSSKLE RIQAQLLSRF
//
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