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Database: UniProt
Entry: A0A1G0NKF3_9PROT
LinkDB: A0A1G0NKF3_9PROT
Original site: A0A1G0NKF3_9PROT 
ID   A0A1G0NKF3_9PROT        Unreviewed;       195 AA.
AC   A0A1G0NKF3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=A2580_00660 {ECO:0000313|EMBL:OGU23951.1};
OS   Hydrogenophilales bacterium RIFOXYD1_FULL_62_11.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1798415 {ECO:0000313|EMBL:OGU23951.1, ECO:0000313|Proteomes:UP000179278};
RN   [1] {ECO:0000313|EMBL:OGU23951.1, ECO:0000313|Proteomes:UP000179278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGU23951.1}.
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DR   EMBL; MGZO01000026; OGU23951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0NKF3; -.
DR   Proteomes; UP000179278; 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:SF25; SCO1 PROTEIN HOMOLOG; 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}.
FT   DOMAIN          38..194
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        77..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   195 AA;  21660 MW;  645ACF9F5BB07D7F CRC64;
     MLATLALGLA PFPAAIAQEH EHHHHHAMPS EQDGYVRTQA TYTIPDVKLL DANRAGVLLR
     SQLDDKPVIL NFIFTSCGAI CPVMSTTFSQ VQAALGQERD TVRMVSISID PEHDTPEALK
     IYAKKYGAGP QWKLLTGSLD NSIAVQRAFD VYRGDKMGHT PATFLRARAG QPWVRLDGFA
     SAEDILREYR QLTFR
//
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