ID A0A0D2B8K0_9EURO Unreviewed; 217 AA.
AC A0A0D2B8K0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_05318 {ECO:0000313|EMBL:KIW15273.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15273.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW15273.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15273.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) 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; KN847495; KIW15273.1; -; Genomic_DNA.
DR RefSeq; XP_016235489.1; XM_016379662.1.
DR AlphaFoldDB; A0A0D2B8K0; -.
DR STRING; 91928.A0A0D2B8K0; -.
DR GeneID; 27332401; -.
DR VEuPathDB; FungiDB:PV08_05318; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:InterPro.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IEA:InterPro.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
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 PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR037736-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037736-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 154
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 62..66
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 217 AA; 24841 MW; DB33AD8879BC7C2B CRC64;
MVFYFQYEKA RLERKRLTEM SKGYGKPKVG GPFTLKDLEG NEFTEKDLLG KYSMIYFGFS
HCPDICPDEL DKLGDAIDII QEKAPNCMRP IFISCDPNRD TPEVLRKYLA EFHPAIQGLS
GTWEQTKNVC KQYRVYFSTP PNLEPGEEDY LVDHSIYFYV MDPEGDFVEC IGRQDTAESA
AAILLQHVRD WQREGKPLDT TPLPYLAAKK DSTSAAK
//
