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Database: UniProt
Entry: A0A1L9U8I7_ASPBC
LinkDB: A0A1L9U8I7_ASPBC
Original site: A0A1L9U8I7_ASPBC 
ID   A0A1L9U8I7_ASPBC        Unreviewed;       848 AA.
AC   A0A1L9U8I7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Mitochondrial thiamine pyrophosphate carrier 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPBRDRAFT_68674 {ECO:0000313|EMBL:OJJ67958.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ67958.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family.
CC       {ECO:0000256|ARBA:ARBA00037964}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375}.
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DR   EMBL; KV878692; OJJ67958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9U8I7; -.
DR   STRING; 767769.A0A1L9U8I7; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_68674; -.
DR   OMA; QSSKHDY; -.
DR   OrthoDB; 2965755at2759; -.
DR   Proteomes; UP000184499; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
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; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43083:SF6; MANNAN POLYMERASE COMPLEXES SUBUNIT MNN9; 1.
DR   PANTHER; PTHR43083; MANNAN POLYMERASE II; 1.
DR   Pfam; PF03452; Anp1; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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:UP000184499};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        480..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          42..127
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          154..243
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          251..344
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  94373 MW;  D45BD6FF40129FFA CRC64;
     MSSTTAPLLT PTTSGIPEQR SSGNMAEADT PTNTPPKPQS SKHDYKGFVA GVFSGIAKLS
     VGHPFDTIKV RLQTSHEGHF RGPLDCVLQT VRKEGVSGFY KGATPPLVGW MVMDSVMLGS
     LTFYRRLLLE NVFSKPEIRA KMPFTGKQTD LRTLPSFGHG IAGIMAGTTV SFIAAPVEHV
     KARLQIQYSA DKSKRLYSGP IDCVRKMLRT HGIAGLYRGL CATMLFRSFF FFWWGSYDIL
     TRMMKEKTSM SAPTINFWAG GISAQIFWIT SYPSDVVKQR LMTDPMGGAL NDGQRRFQGW
     KDAAVAVYRE RGFRGYWRGF VPCFLRAFPA NAMALVAFEG CCGKQERETR DKSAEVSDES
     SGSACSFSGQ LQSCHGSIPS SPSLLPHPLL VRLKPPRLTL HSILCLFRYV RGPDHPLPDC
     WLKSSLDISP GQIEFRGRLI HRAARSPSPP TRLRTSSTFS LHQHTATMAV ARSMRRTSPI
     TVFLAALLAF GFLCFLLSPS SSAAAAAPVT DSSSQLRRDD AAEHPLSPPT KPFLKSQVVR
     EDGQKAPPPV MNYNLNELSS TSESIKKGER VLILTPLARF YQEFWDNVVK LSYPHELISI
     GFIVPKTKDG NAAVTALEQA ISETQSGPID SRFASISILR QDFDPPIQSQ DEKERHKMSN
     QKARRESMSR ARNSLLFTTL GPSTSWVLWL DSDIVETPAT LIQDLTAHDR PVIVPNCFQR
     YYNKDTKKMD VRPYDFNSWI DSSTAQQLAE MMGPDEILLE GYAEMPTYRT LMAYMANTGS
     PRPSREIELD GVGGTALLVK ADVHRDGAMF PAFPFYHLVE TEGFAKMAKR LGYSIYGLPD
     YFVYHYNE
//
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