ID   A0A178IJJ9_9BACT        Unreviewed;       301 AA.
AC   A0A178IJJ9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=AW736_09725 {ECO:0000313|EMBL:OAM90053.1};
OS   Opitutaceae bacterium TSB47.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM90053.1, ECO:0000313|Proteomes:UP000078486};
RN   [1] {ECO:0000313|EMBL:OAM90053.1, ECO:0000313|Proteomes:UP000078486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSB47 {ECO:0000313|EMBL:OAM90053.1,
RC   ECO:0000313|Proteomes:UP000078486};
RA   Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT   "High potential of lignocellulose degradation of a new Verrucomicrobia
RT   species.";
RL   Submitted (JAN-2016) 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:OAM90053.1}.
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DR   EMBL; LRRQ01000075; OAM90053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178IJJ9; -.
DR   STRING; 1184151.AW736_09725; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000078486; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 2.40.50.320; Copper binding periplasmic protein CusF; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR021647; CusF_Ec.
DR   InterPro; IPR042230; CusF_sf.
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:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR   Pfam; PF11604; CusF_Ec; 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:UP000078486}.
FT   DOMAIN          130..297
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         168
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         174
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         261
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        168..174
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   301 AA;  32507 MW;  593CE4471FF41986 CRC64;
     MSTRFLFFLF AGLPVCAWAL LSGSGTLFAA REKERERVFD VTGIVRARLD DGQLVIAHDE
     IPGYMGAMTM AFTPAGPEEA AGVAVNDRVR FRLRVNGGRS RAEAFVVTGR AAAPGKPATS
     SQGGARRGRL REGDAVPAFS LFDERGQPLT AEALRGRLTI VTFIFTRCPV PEYCPAISRK
     FDQLQPAVRK GLPAESAAKV RLLSITLDPE FDRPDILKAY GEAMGADPAI WNFATGEKAE
     IDALVKAFAV YRENNGVTLD HTLATALIGP DGRVADIWRG NGWTVDEVIA SLRKAANVTG
     R
//