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Database: UniProt
Entry: A0A099P573_PICKU
LinkDB: A0A099P573_PICKU
Original site: A0A099P573_PICKU 
ID   A0A099P573_PICKU        Unreviewed;      1616 AA.
AC   A0A099P573;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=JL09_g1458 {ECO:0000313|EMBL:KGK39362.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK39362.1, ECO:0000313|Proteomes:UP000029867};
RN   [1] {ECO:0000313|Proteomes:UP000029867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX   PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL   Microb. Cell Fact. 13:121-121(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KGK39362.1}.
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DR   EMBL; JQFK01000009; KGK39362.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:C5L36_0B09460; -.
DR   VEuPathDB; FungiDB:C5L36_0B09470; -.
DR   VEuPathDB; FungiDB:C5L36_0B09480; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   eggNOG; KOG0764; Eukaryota.
DR   eggNOG; KOG4476; Eukaryota.
DR   HOGENOM; CLU_243709_0_0_1; -.
DR   Proteomes; UP000029867; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0006862; P:nucleotide transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd02961; PDI_a_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR018608; Gti1/Pac2.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044712; SLC25A32-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45683:SF2; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED; 1.
DR   PANTHER; PTHR45683; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED-RELATED; 1.
DR   Pfam; PF09729; Gti1_Pac2; 2.
DR   Pfam; PF00153; Mito_carr; 3.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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        603..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        668..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        778..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1566..1587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          599..697
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          704..806
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          829..921
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   DOMAIN          899..1045
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          110..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1616 AA;  184721 MW;  3332A0BAC52BD48D CRC64;
     MVMRNKTPVS ATYHGYIASS RDALLVIDAV LRGLLLPVTN RPTPKERKAL IRSGNVFVFI
     EEESNIKRWT DGTSWSPSRI LGRFLIYREL SKNIVKDSNN NLSAITSVVE DNGDSNNMDN
     GNASGSRATS TATNNNNNNN NSSTNNNGAN NHYASTESRF VKLNCQPITA YAMAGGEDVI
     RKRSIDDVIK EDANSNNNNN NNNNTDTNST HNSIRGDTTI SNTNEINTNL LNSNIEVDVL
     SDNIYRSDGL IKKSLSIVLH SPSRKTIHLV SYYTTKDVIN DKLNIPSSDN FFKDNSVVPS
     YELIDSLLNT SLGHSISHRR RSDPSSGPIS FLDTDGFDDQ TVMSYTNHKR RRLSEQRQQQ
     QQQQQQQQQQ LQQLQQQQQQ QQQHNKINNN NNNNSSSSIN IINRFRCNCL NNFTLLTHTP
     RTSYDEHAVP SMPVLRSASH PGFDTLPLSH DFQQPQQTAS VTQTHQYHQH HPQQQQQQQQ
     LATAAPPLSQ QLDYPTSLRT LPVSQSSQMQ QNDQLQFNAS PLVNETDDIS NQNKHPQSTL
     ESSNLLTLSS EDSIHSHGCD CEPPKTHQIS TDISVHAVPV LEPLSTHKND LRAFKLRLSP
     NEITSISGAL AGFISGLVVC PLDVAKTRFQ AQGAYNNSND IDKKKILPIL MSAVQSIKLI
     WKEEGFRGLY RGVVPITLGY FPTWMIYFTC YEHFKKFYNN YIHDDNLSYF ASAISSGAIS
     TTLTNPIWVV KTRLMLQMDD GKTVYSSSNV NANTSTNVTR NGDFDAFKKM YQHEGLNVFY
     RGLLPSYFGL IHVAIQFPLY ENFKKILKIS NNGDETLDMS NTSTKMKTLN FLKFILASSL
     SKMIASAITY PHEILRTRLQ LFNNNSNQQN ESQLKGLKRV FKNIIKVEGF KGFYSGFIIN
     LARTVPASAV TMVSFEYFRE YFQSANENES SNDLQSRVPP PLTLSNFDNT LLKGFHMVEF
     YSPYCHHCQN LFPTWVEFYE SNPESSGYAI HQVDCVVSGD LCDREGIRYF PMIRFYGPNS
     KLLASMTSSS RTIDTLNEFA NEQLLIWNEE GDSKFNEDDF VGLQNSMIDN SELRKVLSGD
     LEVPKLISFW PTSNDQLNDS NFQNKYNAHA IFKNSENLYN FRNIWNFVIR NLHKFGEEHK
     LEFHYVNCKS NAALCGSLGF SELLNSNLKN LTPRIVLYLP KSNGNSLFLK PSLIKNRKFN
     HIVKFITNWT YRNLINSELQ DLKINDIKNF IGATTKLKDK NDISDIPNYS KVAFIQVNDP
     NTQVLEDDII LDHLLQPVAD LDSEVYLFKS TDKDGALKLL QDQERNLIDY IKIDEQSLQD
     KISEKLFISR TRSTFPMFIA LKSSSLYTPV YQSFTSKEIR DTKKVLSFIR SNYLPMINHL
     SDDNKYQVFP KRMSPLNSKT EKILVSITDF QPKQFFEVEF YMSKVYHKFQ YLRNMKIFQK
     IDKQRNEKHE EVNRMKLNDA TSDDIIDKLR EKITESYIST DNNLFPVYLD LDTLSKVASS
     LNWNKLDIQK YKVGDSILIS RFTGQYWDQD LRGRQLNIEN IDETVNLLKD ILKNKNSGKS
     ITRQSILLTI FQVWILLLVI AACLHYYKRF QIKRAQQNEK MKGLGILGLS ADSKFD
//
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