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Database: UniProt
Entry: A0A0M9ZND8_9ACTN
LinkDB: A0A0M9ZND8_9ACTN
Original site: A0A0M9ZND8_9ACTN 
ID   A0A0M9ZND8_9ACTN        Unreviewed;       216 AA.
AC   A0A0M9ZND8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=ADL00_18865 {ECO:0000313|EMBL:KOV65658.1};
OS   Streptomyces sp. AS58.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV65658.1, ECO:0000313|Proteomes:UP000037758};
RN   [1] {ECO:0000313|EMBL:KOV65658.1, ECO:0000313|Proteomes:UP000037758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS58 {ECO:0000313|EMBL:KOV65658.1,
RC   ECO:0000313|Proteomes:UP000037758};
RA   Noorani M.;
RL   Submitted (JUL-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:KOV65658.1}.
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DR   EMBL; LGDU01000186; KOV65658.1; -; Genomic_DNA.
DR   RefSeq; WP_053759348.1; NZ_LGDU01000186.1.
DR   AlphaFoldDB; A0A0M9ZND8; -.
DR   PATRIC; fig|1519489.3.peg.4275; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000037758; 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: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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000037758};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..216
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038835210"
FT   DOMAIN          48..205
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         87
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         91
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         176
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        87..91
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   216 AA;  22815 MW;  6EA6267625F62D08 CRC64;
     MRKKTFAAAA LLAAATLTLS ACGSGDDSGS PITVVSEEPG SDKAATVLDQ PFEKPDLVLT
     DTRGKAYDLR EETAGKPTLI YFGYTNCPDV CPLTMNNIAV AKKQLSEAEQ DKLQVVFVTT
     DPERDTASAL GKWLKGIDPQ AVGLTGDFST IQAGARSLGI SIDPPKKEKG KIVSTHGTQV
     IAFSPETDAG YVVYGEEATV DDYTKDLPKL VTGEAP
//
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