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Database: UniProt
Entry: A0A366MDZ3_9EURY
LinkDB: A0A366MDZ3_9EURY
Original site: A0A366MDZ3_9EURY 
ID   A0A366MDZ3_9EURY        Unreviewed;        81 AA.
AC   A0A366MDZ3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative Thioredoxin {ECO:0000313|EMBL:RBQ24478.1};
GN   ORFNames=ALNOE001_01250 {ECO:0000313|EMBL:RBQ24478.1};
OS   Methanobrevibacter sp. NOE.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=2006182 {ECO:0000313|EMBL:RBQ24478.1, ECO:0000313|Proteomes:UP000253099};
RN   [1] {ECO:0000313|EMBL:RBQ24478.1, ECO:0000313|Proteomes:UP000253099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOE {ECO:0000313|EMBL:RBQ24478.1};
RA   Lind A.E., Lewis W.H., Spang A., Guy L., Embley M.T., Ettema T.J.G.;
RT   "Genomic insight into two independent archaeal endosymbiosis events.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007787}.
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:RBQ24478.1}.
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DR   EMBL; NIZT01000003; RBQ24478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366MDZ3; -.
DR   Proteomes; UP000253099; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR004502; Thio_glut.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR00411; redox_disulf_1; 1.
DR   PANTHER; PTHR37170:SF1; GLUTAREDOXIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR37170; GLUTAREDOXIN-RELATED; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253099};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          1..81
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   81 AA;  8798 MW;  308003EF25597E80 CRC64;
     MLKVEVFTSP SCPYCPMAEQ VVDEAKKEIG KGMEVEVVNI MTDRQRAVDY GILAVPAIAI
     NGVVEFVGAP TQEELMAKLK A
//
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