ID   A0A093IY68_EURHL        Unreviewed;       176 AA.
AC   A0A093IY68;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Protein SCO1, mitochondrial {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=N326_10542 {ECO:0000313|EMBL:KFW07695.1};
OS   Eurypyga helias (Sunbittern) (Ardea helias).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC   Eurypygidae; Eurypyga.
OX   NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW07695.1, ECO:0000313|Proteomes:UP000054232};
RN   [1] {ECO:0000313|EMBL:KFW07695.1, ECO:0000313|Proteomes:UP000054232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW07695.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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; KK571504; KFW07695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093IY68; -.
DR   Proteomes; UP000054232; Unassembled WGS sequence.
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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF4; PROTEIN SCO1 HOMOLOG, MITOCHONDRIAL; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054232}.
FT   BINDING         48
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         52
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         139
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        48..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW07695.1"
FT   NON_TER         176
FT                   /evidence="ECO:0000313|EMBL:KFW07695.1"
SQ   SEQUENCE   176 AA;  19976 MW;  B62FDFCFB91AFD23 CRC64;
     ELKKERNRGI GKPLLGGPFS LVSHEGQPKT SKDYIGQWVL IYFGFTHCPD ICPDELEKMI
     EVVDEIDRIP SLPNLTPLFI TIDPERDNEE AIAKYVKEFS PKLIGLTGTK AQIDQVAKAY
     RVYYSEGPKD EDSDYIVDHT IIMYLLGPDG DFVEYYGQNK RSAEISASIA AHMRKY
//