ID   A0A0V1LL82_9BILA        Unreviewed;       301 AA.
AC   A0A0V1LL82;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Protein SCO2-like protein, mitochondrial {ECO:0000313|EMBL:KRZ60287.1};
GN   Name=Sco2 {ECO:0000313|EMBL:KRZ60287.1};
GN   ORFNames=T02_15968 {ECO:0000313|EMBL:KRZ60287.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60287.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ60287.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60287.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ60287.1}.
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DR   EMBL; JYDW01000030; KRZ60287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1LL82; -.
DR   Proteomes; UP000054721; 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:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 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:UP000054721}.
FT   BINDING         157
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         161
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         255
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        157..161
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   301 AA;  34160 MW;  3F646F1324EC3D64 CRC64;
     MMQKLPDFEI ARKAWMNEQL GFFAHMTSTN SSSGEKIKIS TIEFQIESLQ ASVKLNVKIT
     YGNLSVSVPA KITAHAAVFV KPRTCILCQV CEFSEMKRNL GPRTLMKGVM INLEKKRIIG
     KSLIGGSWEL VNHYGQPVKS EDFKGQWLLI YFGFTHCPDV CPDEIEKMCK IISILDKDKE
     FAIVKPLFVS VDPERDDPAA FALISLLHLR HTVEFSPKLL GLTGSEEQVN KICKAFRVYR
     SQGPRDQDDD YIVDHTIIMY LINPDGAFVD YYGQSRNAEE IANAIRAKMI IYESQLKLRG
     K
//