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Database: UniProt
Entry: T1J9I2_STRMM
LinkDB: T1J9I2_STRMM
Original site: T1J9I2_STRMM 
ID   T1J9I2_STRMM            Unreviewed;       236 AA.
AC   T1J9I2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR010379-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR010379-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- FUNCTION: Copper metallochaperone essential for the synthesis and
CC       maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved
CC       in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a
CC       thiol-disulfide oxidoreductase to regulate the redox state of the
CC       cysteines in SCO1 during maturation of MT-CO2/COX2.
CC       {ECO:0000256|PIRNR:PIRNR037736}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037736}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|PIRNR:PIRNR037736}.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996, ECO:0000256|PIRNR:PIRNR037736}.
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DR   EMBL; JH431975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1J9I2; -.
DR   STRING; 126957.T1J9I2; -.
DR   EnsemblMetazoa; SMAR010379-RA; SMAR010379-PA; SMAR010379.
DR   eggNOG; KOG2792; Eukaryota.
DR   HOGENOM; CLU_050131_0_3_1; -.
DR   OMA; NGEFVDY; -.
DR   OrthoDB; 169656at2759; -.
DR   PhylomeDB; T1J9I2; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:UniProtKB-UniRule.
DR   GO; GO:0008535; P:respiratory chain complex IV assembly; IEA:InterPro.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   PIRSF; PIRSF037736; SCO1; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|PIRNR:PIRNR037736};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRNR:PIRNR037736};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037736};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR037736};
KW   Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR037736};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..226
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         100
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         191
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   DISULFID        100..104
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   236 AA;  27174 MW;  6474E7FCED336AEF CRC64;
     MRRVSQLSRN YQKATKEKEK EWPITWKSLF VTFAIGGAIT GGVMYVRREK EMKIERERRR
     VLGKASIGGH FDLIDHNGKP CSSRDFFGKW ILLYFGFTHC PDICPDEIEK MVNVVDSLEK
     NPNLAPVQPL FISVDPDRDS VPVVAGYIKE FSPKLIGLTG TQEQINKVAK SFRVYYSAGP
     KDVDADYIVD HTIIIYLIDP EGRFVDYYGQ TRTYEQVADA VQLQMLKYES LKSKWF
//
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