ID A0A0X3NTG3_SCHSO Unreviewed; 178 AA.
AC A0A0X3NTG3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein SCO1 homolog {ECO:0000313|EMBL:JAP40777.1, ECO:0000313|WBParaSite:SSLN_0001535301-mRNA-1};
GN Name=SCO1 {ECO:0000313|EMBL:JAP40777.1};
GN ORFNames=SSLN_LOCUS14794 {ECO:0000313|EMBL:VDM01180.1}, TR93178
GN {ECO:0000313|EMBL:JAP40777.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|EMBL:JAP40777.1};
RN [1] {ECO:0000313|EMBL:JAP40777.1}
RP NUCLEOTIDE SEQUENCE.
RA Hebert F.O., Grambauer S., Barber I., Landry C.R., Aubin-Horth N.;
RT "Reference transcriptome for the parasite Schistocephalus solidus: insights
RT into the molecular evolution of parasitism.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SSLN_0001535301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDM01180.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDM01180.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; GEEE01022448; JAP40777.1; -; Transcribed_RNA.
DR EMBL; UYSU01039317; VDM01180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3NTG3; -.
DR STRING; 70667.A0A0X3NTG3; -.
DR WBParaSite; SSLN_0001535301-mRNA-1; SSLN_0001535301-mRNA-1; SSLN_0001535301.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; 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 InterPro; IPR013766; Thioredoxin_domain.
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.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275846}.
FT DOMAIN 8..173
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 50
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 46..50
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 178 AA; 20457 MW; E71BB7A4C8FCC2DF CRC64;
MKNIAEGLSQ MAIGGEFRLI DQKGMELTLA DFRGKWLLIY FGFCRCPDIC PEQLERLVEI
HERLALYGKD KDFVPIFITV DPERDTPEVV GEYCKEFSPK LVGLTGSREQ INMVAKRYHI
YHSQGPKDSD GDYIVDHTVV MYLIGPNGEF VDYYGQVKPL NEIVRSIMNR MKARATEK
//
