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Database: UniProt
Entry: A0A317VFJ3_9EURO
LinkDB: A0A317VFJ3_9EURO
Original site: A0A317VFJ3_9EURO 
ID   A0A317VFJ3_9EURO        Unreviewed;       549 AA.
AC   A0A317VFJ3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Mitochondrial carrier {ECO:0000313|EMBL:PWY71642.1};
GN   ORFNames=BO70DRAFT_389509 {ECO:0000313|EMBL:PWY71642.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY71642.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY71642.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY71642.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-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:PWY71642.1}.
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DR   EMBL; MSFL01000027; PWY71642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VFJ3; -.
DR   STRING; 1448321.A0A317VFJ3; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_389509; -.
DR   OrthoDB; 5472853at2759; -.
DR   Proteomes; UP000247233; 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; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044677; SLC25A3/Pic2/Mir1-like.
DR   PANTHER; PTHR45671:SF13; PHOSPHATE TRANSPORTER PIC2, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12080)-RELATED; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000247233};
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          1..83
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          93..178
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          194..278
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          281..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..330
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        423..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  60014 MW;  655D7309F7E7A4E9 CRC64;
     MATQKTNYPL GKIEPDSARY FASCTLGGIV VDPKIYTSNL SAWRTIMSKE GLRGIFFGWT
     PTFVGYSMQG AGKYGFYEYF KYLYGDNLFP NANRTVVFLG ASASAEFFAD IALCPMEAIK
     VRMQTTLPPF AHSLREGWGK VVAKEGISGL YKGLYPLWAR QIPYTMTKFA TFEETVKYIY
     KTLGKPKESY NGLQQTGVSF LGGYIAGIFC AIVSHPADVM VSKLNADRKA GEGAMTAVSR
     IYGNIGFSGL WNGLPVRIVM LGTLTGFQWL MISSYDSFKP PPSTMDETTT RQPSSTSNPP
     SVENAYKRKC LALKKRLNEI EDENELMRVR NRRGWQYIQK MRLESCILLE RLSKVTGMTE
     EAQAGVNPEL RARAAAMMTT ISSMNGAEAK NGADGAGASA NPGGLYLEDE TEGSSDEQPP
     TPQERPLRVK RSRKSNLPND PGAEDEGPNT NTNDNTNNGN ENKTNNGNAP ESGPDSAAGL
     PRLAPAPSQE DMTSSFRIQT GSNGSPVHDK EGSDRGSNQP ESGRAGEAAA EKSTTPMDMD
     KERDEEREA
//
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