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Database: UniProt
Entry: A0A091V9D8_NIPNI
LinkDB: A0A091V9D8_NIPNI
Original site: A0A091V9D8_NIPNI 
ID   A0A091V9D8_NIPNI        Unreviewed;       166 AA.
AC   A0A091V9D8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=SCO1 protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=Y956_15144 {ECO:0000313|EMBL:KFQ98997.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ98997.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFQ98997.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ98997.1};
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; KL410730; KFQ98997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091V9D8; -.
DR   STRING; 128390.A0A091V9D8; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   Proteomes; UP000053283; 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:UP000053283};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..166
FT                   /note="SCO1 protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001883019"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        77..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ98997.1"
FT   NON_TER         166
FT                   /evidence="ECO:0000313|EMBL:KFQ98997.1"
SQ   SEQUENCE   166 AA;  18836 MW;  D041C91D40D9D596 CRC64;
     VSWRSLAATF VLCGGLLAGM KKVKRWKEEE LEKERNRGIG KPLLGGPFSL VSHEGQPKTS
     KDYIGQWVLI YFGFTHCPDI CPDELEKMIE VVDEIDRIPS LPNLTPLFIT IDPERDDEEA
     IARYVKEFSP KLIGLTGTKA QIDQVAKAYR VYYSEGPKDE DNDYIV
//
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