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Database: UniProt
Entry: A0A166TTH9_9PEZI
LinkDB: A0A166TTH9_9PEZI
Original site: A0A166TTH9_9PEZI 
ID   A0A166TTH9_9PEZI        Unreviewed;       315 AA.
AC   A0A166TTH9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE   AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN   ORFNames=CT0861_01421 {ECO:0000313|EMBL:KZL72468.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL72468.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL72468.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL72468.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL72468.1}.
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DR   EMBL; LFIV01000058; KZL72468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166TTH9; -.
DR   STRING; 708197.A0A166TTH9; -.
DR   OrthoDB; 1330359at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368008};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   TRANSMEM        116..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        220..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          13..106
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          118..210
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          218..304
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   315 AA;  34089 MW;  1796A072503D69FF CRC64;
     MSPPTDQKVL GMPPFVADFL MGGVSAAVSK TAAAPIERIK LLIQNQDEML KQGRLDRKYD
     GIVDCFKRTA ADEGVMSLWR GNTANVIRYF PTQALNFAFR DKFKKMFGFK KERDGYAWWM
     AGNLASGGAA GATSLLFVYS LDYARTRLAN DAKSAKKGGE RQFNGLVDVY RKTLASDGIA
     GLYRGFMPSV AGIVVYRGLY FGLYDSIKPV VLTGNLANNF LASFALGWCV TTAAGIASYP
     LDTIRRRMMM TSGEAVKYKS SFDAGKQIIA KEGVKSLFKG AGANILRGVA GAGVLSIYDQ
     LQVLLFGKAF KGGSG
//
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