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Database: UniProt
Entry: A0A401KFI0_ASPAW
LinkDB: A0A401KFI0_ASPAW
Original site: A0A401KFI0_ASPAW 
ID   A0A401KFI0_ASPAW        Unreviewed;       379 AA.
AC   A0A401KFI0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Mitochondrial phosphate carrier protein 2 {ECO:0000313|EMBL:GCB18083.1};
GN   ORFNames=AAWM_00968 {ECO:0000313|EMBL:GCB18083.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB18083.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB18083.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB18083.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       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: 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:GCB18083.1}.
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DR   EMBL; BDHI01000001; GCB18083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401KFI0; -.
DR   STRING; 105351.A0A401KFI0; -.
DR   Proteomes; UP000286921; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044677; SLC25A3/Pic2/Mir1-like.
DR   PANTHER; PTHR45671:SF10; PHOSPHATE CARRIER PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45671; SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER PHOSPHATE CARRIER), MEMBER 3, LIKE-RELATED-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
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:UP000286921};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   REPEAT          82..166
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          179..264
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          280..364
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  41285 MW;  0EE91846DEDD3961 CRC64;
     MFPSEGDIAR AFASQSPLGQ PQQIQKPEAA GLKRRQPFPA WNVIEDIEKK ADAIAKEASR
     EFDVASQKAQ AKTGKIEPWT PKYYAACTVG GMLACGLTHT AVTPLDLIKC RRQVDPLLYK
     SNAEAFRTIR GAEGLRGVFT GWGPTFFGYS AQGAFKYGGY EFFKKFYSDL VGVENATRWK
     TSLYLTASAS AELIADVALC PFEAVKVRMQ TTIPPDIRST FTGISSVVNK EGVAGLYKGL
     YPLWGRQIPY TMMKFASFET IVEMIYNTLP GQKSDYNKGA QTAVAFTGGY LAGILCAVVS
     HPADVMVSKL NANRQAGEAF GAAMSRIYKD IGFGGLWNGL PVRIVMIGTL TGLQWMIYDS
     FKIFMGLPTT GGGPPAEKK
//
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