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Database: UniProt
Entry: A0A0S8ATI5_9BACT
LinkDB: A0A0S8ATI5_9BACT
Original site: A0A0S8ATI5_9BACT 
ID   A0A0S8ATI5_9BACT        Unreviewed;       148 AA.
AC   A0A0S8ATI5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:KPK01978.1};
GN   ORFNames=AMK71_03830 {ECO:0000313|EMBL:KPK01978.1};
OS   Nitrospira bacterium SG8_35_4.
OC   Bacteria; Nitrospirota; Nitrospiria.
OX   NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPK01978.1, ECO:0000313|Proteomes:UP000050997};
RN   [1] {ECO:0000313|EMBL:KPK01978.1, ECO:0000313|Proteomes:UP000050997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPK01978.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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:KPK01978.1}.
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DR   EMBL; LJTM01000045; KPK01978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8ATI5; -.
DR   Proteomes; UP000050997; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR049299; Thio2_N.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF40; THIOREDOXIN 2; 1.
DR   Pfam; PF21352; Thio2_N; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          33..145
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   148 AA;  16577 MW;  D224DB0E5248440F CRC64;
     MSKTIHIVCP NCKSTNRLPE LRLSSNPRCG RCKQNLFSAH TVELTHYDFH RHISSNQIPV
     VVDFWASWCG PCKIMSPILE QAAAYLEPNV RVAKVNTETE QGLAAKFNIR SIPTIIIFKN
     GNEASRQSGA MDLATLIQWV RTNALGLE
//
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