ID A0A2T3AGJ9_9PEZI Unreviewed; 689 AA.
AC A0A2T3AGJ9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Mitochondrial thiamine pyrophosphate carrier 1 {ECO:0000256|ARBA:ARBA00021935};
GN ORFNames=BD289DRAFT_480181 {ECO:0000313|EMBL:PSR97333.1};
OS Coniella lustricola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR97333.1, ECO:0000313|Proteomes:UP000241462};
RN [1] {ECO:0000313|EMBL:PSR97333.1, ECO:0000313|Proteomes:UP000241462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR97333.1,
RC ECO:0000313|Proteomes:UP000241462};
RA Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT "Coniella lustricola, a new species from submerged detritus.";
RL Mycol. Prog. 17:191-203(2018).
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}.
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DR EMBL; KZ678392; PSR97333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AGJ9; -.
DR STRING; 2025994.A0A2T3AGJ9; -.
DR InParanoid; A0A2T3AGJ9; -.
DR Proteomes; UP000241462; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR24089:SF57; FI05451P; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000241462};
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}.
FT DOMAIN 58..93
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 97..124
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 125..160
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 386..476
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 489..578
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 596..685
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 216..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 74831 MW; 68A6B466E22EC926 CRC64;
MQLPQAVTEL EMDLAESQNQ RDKRVEELWR KLAPQGTNEL DLKGLQKGLR RIDHPLKNAD
DMMKDIIQMV DSNQDGKIQY EEFRVFVEAA ERQLHLLFTS IDRDHDGRVG PDELAAAFRK
AGLTVPKRRL LGFFDEIDFN HDGYISFDEW RDFLLFMPSS HGSPLEAALS YYNTVVMINA
EGDSMVTEDT LEGLGTTGFL LQALFGSILR LAQPTPPQQP PYLNPPHLDG VSCGPDPVSS
TATTASTSQP DPTTRQRQPR TSSQLKPPLP LADDTTTSND IYPATTTSPS RISAAYSSQY
SQSAIESISG ISPTAASMAQ RDAGSQPPLI NPSGTSDGYV GGGAEFLSIH DHDPDSSSQL
YSSDFSLDGH EYEIEQDTKS GLTQYLPEPG YFVAGAVAGG VSRTATAPLD RIKVALLVAT
GAKSGSAEAK SITSAVHELY KAGGLRTFFA GNGLNVLKIM PETAIKFGSY EAAKRTLATL
EGHSDPTKIN PFSKFAAGGV AGMAAQACVY PVDTLKFRLQ CETVQGGPTG NALLVQTARK
MMTEGGFRSA YRGLTMGLIG MFPYSAIDMG TFELLKKTYT RHKAHYYGIH EEDAAPGNMI
TGIMGAFSGA FGATAVYPIN VMRTRLQTQG TRMHPPTYTG IWDVTAKTWK NEGMRGMYKG
LVPNLLKVAP ALSITWVVYE SSKKAMDLH
//
