ID   A0A078AQ93_STYLE        Unreviewed;       312 AA.
AC   A0A078AQ93;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDW84570.1};
GN   Name=Contig6687.g7154 {ECO:0000313|EMBL:CDW84570.1};
GN   ORFNames=STYLEM_13635 {ECO:0000313|EMBL:CDW84570.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW84570.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW84570.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW84570.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CCKQ01012938; CDW84570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078AQ93; -.
DR   EnsemblProtists; CDW84570; CDW84570; STYLEM_13635.
DR   InParanoid; A0A078AQ93; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         135
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         256
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        131..135
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   312 AA;  36265 MW;  BDB0B117C16D7093 CRC64;
     MFSEQPNNSN KSKRDSFEQK EREKVSKAPE MDSKEDVSFQ DNYTGIRVLL FGVCVVFSGY
     FIHTKMQNLQ RLNKLKQQGL IDYNDESKLS EEEKKIRIGG YWALKDLEGK DFSSYKLEGS
     YYLLFFGFSL CPDVCPLSIL KMTKAINKIR TSNEGKFFRL KPVFVTVNPD YDTPQKLDQF
     KQMFDEHLIV LRAESTQSPQ LMEMLRKFKV PVGLSPDEVV KVNEFFSEKH EKKGFFSRIF
     SKKENLDSDM GYMNDHSRVF YLIGPENQFL SFYNLDIETN ELSASIMDDM SYDLGTRYVG
     TGHKPPVKLG QQ
//