ID W2SBK0_9EURO Unreviewed; 217 AA.
AC W2SBK0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_00162 {ECO:0000313|EMBL:ETN45980.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45980.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN45980.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45980.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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; KB822711; ETN45980.1; -; Genomic_DNA.
DR RefSeq; XP_008710692.1; XM_008712470.1.
DR AlphaFoldDB; W2SBK0; -.
DR STRING; 1220924.W2SBK0; -.
DR GeneID; 19967501; -.
DR VEuPathDB; FungiDB:HMPREF1541_00162; -.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; W2SBK0; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000030752; 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:UP000030752}.
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; 24962 MW; 1F1F1EF637499569 CRC64;
MIFYFQYEKQ RLERKRIVEM SKGYGKPKVG GPFQLRDVDG KEYTEKDLLG KYTLIYFGFT
HCPDICPDEL DKMSEAIDII QKQAPNALRS IFVSVDPARD SPEVLRSYVD EFHPSLIGLT
GTWQQVKEMC KQYRVYFSTP AELKPGEEDY LVDHSIYFYV MDPEGDFVEC IGRQDTPESA
AGIVLQHIKD WKREGKPIDT TPLPYLTQKA AVAVTRA
//
