ID   A0A091N4A5_9PASS        Unreviewed;       184 AA.
AC   A0A091N4A5;
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=N310_03492 {ECO:0000313|EMBL:KFP84628.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP84628.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP84628.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP84628.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK842366; KFP84628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091N4A5; -.
DR   Proteomes; UP000053537; 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:UP000053537}.
FT   BINDING         56
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         60
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         147
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        56..60
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP84628.1"
FT   NON_TER         184
FT                   /evidence="ECO:0000313|EMBL:KFP84628.1"
SQ   SEQUENCE   184 AA;  20973 MW;  958E132949942833 CRC64;
     VVKRRKEEAL EKERNRGIGK PLLGGPFSLV SHEGQPRTSK DYLGQWVLIY FGFTHCPDIC
     PDELEKMVAV VDEIDRIPSL PNLTPLFITI DPERDSQEAI ARYVKEFSPK LVGLTGTRAQ
     IDQVAKAYRV YYSEGPKDED NDYIVDHTII MYLLGPDGDF VDYYGQNKRS TEISASIASH
     MRKY
//