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Database: UniProt
Entry: A0A1W0A0J9_9STRA
LinkDB: A0A1W0A0J9_9STRA
Original site: A0A1W0A0J9_9STRA 
ID   A0A1W0A0J9_9STRA        Unreviewed;      1298 AA.
AC   A0A1W0A0J9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Mitochondrial Carrier (MC) Family {ECO:0000313|EMBL:OQS03822.1};
GN   ORFNames=THRCLA_03885 {ECO:0000313|EMBL:OQS03822.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS03822.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQS03822.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS03822.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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}.
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:OQS03822.1}.
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DR   EMBL; JNBS01000756; OQS03822.1; -; Genomic_DNA.
DR   STRING; 74557.A0A1W0A0J9; -.
DR   OrthoDB; 52111at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:InterPro.
DR   CDD; cd14686; bZIP; 1.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR045315; Mtm1-like.
DR   PANTHER; PTHR45760; FI19922P1-RELATED; 1.
DR   PANTHER; PTHR45760:SF2; FI19922P1-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 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}; Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}.
FT   REPEAT          964..1107
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          1115..1201
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          1210..1294
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   COILED          66..93
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1298 AA;  145990 MW;  4FE10FD24BB93CCA CRC64;
     MDFCLIPHPH RYVHYDVRIS ELEMNTIDVG ISVDWTAEEA SILDTLLSSP KPSKADKHRV
     VLARYRKRKR DELLQLRCTA SELEARLTHL QELHQLEDLE HPPSKWQKLA NKERQREMAA
     MAENAQLRDL VRNQLVTAQI FAKLIAKAWE ERSSTMPMDL EEDKWKSLHL VADPTLRAAG
     MVNILDRERA NVESAFIEAG LIDVEADFQK HISKCIPDTP HEFQNVVYRH TRLPLKYVAE
     GVWRCIRGTA GGIPNINRHC TQFVNVDKYT SYVKGWLEHP LGRFQRRVLC KLYFDNEQVT
     EATQCLVVCR SIEQDDVDPY DSNQPYSNEV SWHLLEAAAD GVLKEDRQWT LETMDMLETY
     TCMEIAVLDE SKIPKKLAGI WHHIMLAVGG DSTYLNVIDA HLNATKKKLK NLGEMNMNEN
     GALDQLFVPK FSNVVDPFPE FTENAIPVAL AGFHMVFNPI VPRIIETHNM HDSIVGYAYS
     ASTPELLALK ELELQIVLGR LHNNKRTRVE DGVGHRPTLI VLSSDSLGKD HSPLHNMPIS
     SHLPVDWGYV PHLVEFRRGN VPIVLSIPHG GASSVASILG RWQLNNLTQR SQSKTSTKRF
     TTFADTRTIH VGADASKAFQ MLTDGCQPYL VIAKFHRKYV DVNRAPNEDA YVRDTSLSKH
     IYEKYHSTLL HTIQEIWLRF PMHDPLILDI HGQRAATCPF LGISNVESKQ LVYLGTRNGL
     TIHSMHSLQQ SFVGYLHEAL QDKAWLGVYP LAEQDKEGYW WWEKERKEFL GGFIVRTYGF
     AETNANAIQL EFGASMRGAD VDMHTEESKM LRQRTSEALA IAMASHVQCI DFKHSLDSDF
     TCQRFLQPDA KGYDVSRTAG LALFGLVYYG GPCKSLYLYF DKVMGTKPTP RTVVLQTFID
     CYVHTPIFLI PSFYFITNGV KGKSIEQTTI QLKREWHTAS FGSAGTGPLV NMNASRKPKE
     SVFASSVKKS IAASSGAMMT SLFVTPLDVA KVRLQAQTSN FSTMCATSKS KTACVQHSPR
     ITPCRSMRNP LLAAAPKAPC KFRQMTVHCV QANCHAHQPL SGTFATLRHV FHTEGLRGLY
     AGLPPTLMLA VPSTVLYYTS YDYMVREGKK KFPELSVIMP LLAGSSARIV AATIVSPLEL
     VRTRMQGHGK NFQGNGMWNT LRTAVQQQGF KALYRGLNAT LARDVPFSAI YWTCFEHFRS
     TLEAKFPEST KIEQSFGAGA MAGAIAATLT TPFDVVKTLQ QVDGTMNMST AEVLRRLIHT
     QGPQAIMTGL TPRLAKIVPS CAIMISSYEL GKLYLGID
//
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