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Database: UniProt
Entry: A0A0J1B0W0_9TREE
LinkDB: A0A0J1B0W0_9TREE
Original site: A0A0J1B0W0_9TREE 
ID   A0A0J1B0W0_9TREE        Unreviewed;       434 AA.
AC   A0A0J1B0W0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Cation efflux protein {ECO:0000313|EMBL:KLT41244.1};
GN   ORFNames=CC85DRAFT_297137 {ECO:0000313|EMBL:KLT41244.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41244.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT41244.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41244.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KQ087221; KLT41244.1; -; Genomic_DNA.
DR   RefSeq; XP_018277735.1; XM_018425001.1.
DR   AlphaFoldDB; A0A0J1B0W0; -.
DR   STRING; 879819.A0A0J1B0W0; -.
DR   GeneID; 28985604; -.
DR   OrthoDB; 1218545at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:InterPro.
DR   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 2.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   InterPro; IPR045316; Msc2-like.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45755; -; 1.
DR   PANTHER; PTHR45755:SF4; ZINC TRANSPORTER 7; 1.
DR   Pfam; PF01545; Cation_efflux; 2.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          134..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..155
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..264
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  46940 MW;  B9FD4B9E2990B7F3 CRC64;
     MRTPASRRIF GFLCLNLAYM GVQMGYGIAT NSLGLISDAI HMLFDCLGIG VGLWASVAAT
     WKSDGQYTFG YSRIETLSGF ANGCFLILIS VFIIFEAIQR VLNPPEMETR QLLLVSGIGL
     AINLFGMWAT GGHHHHGHSH GHGHGHGHSH GHGHGHDHGH TNGNGHVHSI VHDKKTDIGG
     AHEHDACSNG HSHGHHEHGH GHDHKVDHGH DVNHGGQCDH AQANGNGLGH AHGHSHVHHA
     HHDHSHSHDH GHAHSHSHGH DAHAHSHSHS HEDHDHDPHH SHNMRGVFLH VMADTLGSVG
     VIVSTLLIRW TGWTGFDPLA SLFIATLILA SVFPLVLDAA RVLVLDVGPY AEPTLRKALG
     DVATVRGVKS YSAARVWPRE DANLVGSLHI QLAPGAEPEK VAARVEAAMR SRVPGLKELV
     LQIEDERFCT CMTS
//
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