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Database: UniProt
Entry: K5XDJ9_PHACS
LinkDB: K5XDJ9_PHACS
Original site: K5XDJ9_PHACS 
ID   K5XDJ9_PHACS            Unreviewed;       312 AA.
AC   K5XDJ9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE   AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN   ORFNames=PHACADRAFT_247486 {ECO:0000313|EMBL:EKM61107.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM61107.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM61107.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM61107.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930468; EKM61107.1; -; Genomic_DNA.
DR   RefSeq; XP_007390541.1; XM_007390479.1.
DR   AlphaFoldDB; K5XDJ9; -.
DR   STRING; 650164.K5XDJ9; -.
DR   GeneID; 18914096; -.
DR   KEGG; pco:PHACADRAFT_247486; -.
DR   HOGENOM; CLU_015166_12_0_1; -.
DR   InParanoid; K5XDJ9; -.
DR   OrthoDB; 1330359at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
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        178..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368008"
FT   REPEAT          11..104
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          115..207
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          215..301
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   312 AA;  33623 MW;  9508F72C57B6EC2B CRC64;
     MADVKKAKTP KEFAIDFMMG GVSAAVAKTS AAPIERIKLL VQNQDEMIKQ GRLATPYKGV
     ADCFGRTYRD EGLLSLWRGN TANVIRYFPT QALNFAFKDY FKSLFGFKKS EGYWRWFAGN
     VASGGAAGAS SLLFVYSLDY ARTRLANDAK SVKGGGQRQF NGLVDVYKKT LASDGIAGLY
     RGFVPSVVGI IVYRGLYFGV YDSLKPVVLV GALEGSFLAS FFLGWGVTIG AGLASYPLDT
     IRRRMMMTSG AGVHYKSMFD AGSQIIAKEG YKSLFKGAGA NILRGVAGAG VLSLYDKLQQ
     VVFGKVYSGG SG
//
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