ID A0A150VC46_9PEZI Unreviewed; 323 AA.
AC A0A150VC46;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYG48077.1};
GN ORFNames=M433DRAFT_151509 {ECO:0000313|EMBL:KYG48077.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48077.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG48077.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG48077.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG48077.1}.
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DR EMBL; JPDO01000058; KYG48077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VC46; -.
DR STRING; 766039.A0A150VC46; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR049563; TXTP-like.
DR PANTHER; PTHR45788; SUCCINATE/FUMARATE MITOCHONDRIAL TRANSPORTER-RELATED; 1.
DR PANTHER; PTHR45788:SF2; SUCCINATE_FUMARATE MITOCHONDRIAL TRANSPORTER; 1.
DR Pfam; PF00153; Mito_carr; 3.
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:UP000075602};
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 15..105
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 113..207
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 219..308
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 323 AA; 34968 MW; 9CC7A03D2B071BE6 CRC64;
MSAKSTAGPG GKKPPSAATN LIAGGAAGMM EALACHPLDT IKVRMQLSRR ARQPGAKRRG
FIKTGTEIVK KETPLGLYKG LGAVLTGIVP KMAIRFTSYE WYKQLLANRS GQISGGSNFV
AGLMAGITEA VFVVTPMEVV KIRLQAQHHS MADPLDVPKY RNAAHAFYTV LREEGPGALW
RGVSLTALRQ GTNQAANFTA YTELKARLQQ WRGDPSGQLP SWQTSIIGLI SGAVGPFTNA
PIDTIKTRLQ RTPAEPGQTA WGRITAIGSQ MLKQEGVRAF WMGITPRVMR VAPGQAVTFA
TYEYLKDLLE KGRDMIPGGQ YEE
//
