ID A0A162IHK7_9HYPO Unreviewed; 357 AA.
AC A0A162IHK7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Mitochondrial thiamine pyrophosphate carrier 1 {ECO:0000256|ARBA:ARBA00021935};
GN ORFNames=AAL_05289 {ECO:0000313|EMBL:KZZ94322.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ94322.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ94322.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ94322.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- FUNCTION: Mitochondrial transporter that mediates uptake of thiamine
CC pyrophosphate (ThPP) into mitochondria.
CC {ECO:0000256|ARBA:ARBA00002238}.
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:KZZ94322.1}.
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DR EMBL; AZGY01000011; KZZ94322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162IHK7; -.
DR STRING; 1081109.A0A162IHK7; -.
DR OrthoDB; 1330359at2759; -.
DR Proteomes; UP000078544; 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 PANTHER; PTHR24089:SF777; MITOCHONDRIAL SUBSTRATE CARRIER FAMILY PROTEIN A; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 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:UP000078544};
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 53..141
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 151..246
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 255..344
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 38699 MW; BD4C71BA12D7CE18 CRC64;
MSEVKGGSRL PSSPSASTTN VQMQSPTGPA AVARPPQPAD TESFADFREW ISQPVVAAFC
GGGVAGAVSR TVVSPLERLK ILLQVQSVGR DAYKLSVGSA LGKMWKDEGW RGFMRGNGTN
CIRIVPYSAV QFSSYNFYKR NIFEAYPGQD LAPLTRLVCG GIAGITSVFF TYPLDIVRTR
LSIQTASFAE LGSKPAKMPG MWATLIQMYK TEGGMAALYR GIVPTVAGVA PYVGLNFMVY
ESVRKYLTYE GEQNPGAARK LLAGAISGAV AQTFTYPFDV LRRRFQINTM SGMGYQYKGV
VDAVRVIIGQ EGLRGLYKGI VPNLLKVAPS MASSWLSFEM TRDFLVDLKP EVSQAAL
//
