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Database: UniProt
Entry: H9BA02_EIMTE
LinkDB: H9BA02_EIMTE
Original site: H9BA02_EIMTE 
ID   H9BA02_EIMTE            Unreviewed;       309 AA.
AC   H9BA02;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE   AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN   ORFNames=ETH_00011560 {ECO:0000313|EMBL:CDJ41240.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:AET50812.1};
RN   [1] {ECO:0000313|EMBL:AET50812.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Houghton {ECO:0000313|EMBL:AET50812.1};
RX   PubMed=22244352; DOI=10.1186/1471-2164-13-21;
RA   Amiruddin N., Lee X.W., Blake D.P., Suzuki Y., Tay Y.L., Lim L.S.,
RA   Tomley F.M., Watanabe J., Sugimoto C., Wan K.L.;
RT   "Characterisation of full-length cDNA sequences provides insights into the
RT   Eimeria tenella transcriptome.";
RL   BMC Genomics 13:21-21(2012).
RN   [2] {ECO:0000313|EMBL:CDJ41240.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ41240.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CDJ41240.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ41240.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the membrane.
CC       {ECO:0000256|RuleBase:RU368008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024143};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC         Evidence={ECO:0000256|ARBA:ARBA00024143};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU368008}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368008}.
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DR   EMBL; JN987589; AET50812.1; -; mRNA.
DR   EMBL; HG675579; CDJ41240.1; -; Genomic_DNA.
DR   RefSeq; XP_013231990.1; XM_013376536.1.
DR   AlphaFoldDB; H9BA02; -.
DR   EnsemblProtists; CDJ41240; CDJ41240; ETH_00011560.
DR   GeneID; 25251501; -.
DR   VEuPathDB; ToxoDB:ETH2_0507900; -.
DR   VEuPathDB; ToxoDB:ETH_00011560; -.
DR   OMA; AWWMAGN; -.
DR   OrthoDB; 1330359at2759; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002113; ADT_euk_type.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45635; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR45635:SF14; ADP,ATP CARRIER PROTEIN-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00927; ADPTRNSLCASE.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|RuleBase:RU368008};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   TRANSMEM        121..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          14..108
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          120..209
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          217..307
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   309 AA;  33974 MW;  C229A728EF05F9D0 CRC64;
     MAAKESKGGE NALLDAAKNF MAGGVSAGVS KTIVAPIERV KMLIQTQDSI PDIKEGRVPR
     YTGIGNCFVR VSREQGALSL WRGNLANVIR YFPTQAFNFT FKDTFKRIFP KYDQKKEFAK
     FFLANVASGG LAGAASLTVV YPLDFARTRL ASDVGKGAAR EFSGLLDCLQ KVYSRTGFLS
     LYQGFGVSVQ GIVVYRGAYF GLFDTAKAVL FSDKTKSNLF LKWAVAQSVT AAAGVVSYPF
     DTVRRRMMMM AGRRATEDIQ YSSTFDCWAK ILAQEGPRGF FKGAWANVLR GAGAALVLVF
     YDEFQRLLM
//
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