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Database: UniProt
Entry: D4JAF1_9FIRM
LinkDB: D4JAF1_9FIRM
Original site: D4JAF1_9FIRM 
ID   D4JAF1_9FIRM            Unreviewed;       104 AA.
AC   D4JAF1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Thioredoxin {ECO:0000256|ARBA:ARBA00020570, ECO:0000256|PIRNR:PIRNR000077};
GN   ORFNames=CC1_26990 {ECO:0000313|EMBL:CBK81322.1};
OS   Coprococcus catus GD/7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81322.1, ECO:0000313|Proteomes:UP000008798};
RN   [1] {ECO:0000313|EMBL:CBK81322.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81322.1,
RC   ECO:0000313|Proteomes:UP000008798};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Coprococcus catus GD/7.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK81322.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81322.1,
RC   ECO:0000313|Proteomes:UP000008798};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; FP929038; CBK81322.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JAF1; -.
DR   STRING; 717962.CC1_26990; -.
DR   KEGG; cct:CC1_26990; -.
DR   PATRIC; fig|717962.3.peg.2586; -.
DR   HOGENOM; CLU_090389_10_2_9; -.
DR   Proteomes; UP000008798; Chromosome.
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   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; 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   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..104
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   104 AA;  11771 MW;  23E13CFA5FE9FB73 CRC64;
     MMKEFNKRTL DEYAAEGKMV LVEFSAPWCV YCRRLAPAME KIAEEYKDIL TVGSVNIDNE
     QELARQERIE VVPTLVLYKN GQAVDSIVGP GSKAAVEEFI RKNS
//
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