ID R7KTH5_9BACE Unreviewed; 99 AA. AC R7KTH5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 19-FEB-2014, entry version 5. DE SubName: Full=Thioredoxin C-2; GN ORFNames=BN644_03596; OS Bacteroides thetaiotaomicron CAG:40. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263054; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CBJO010000163; CDE79704.1; -; Genomic_DNA. DR ProteinModelPortal; R7KTH5; -. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:GOC. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10438; PTHR10438; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PIRSF; PIRSF000077; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; FT DISULFID 23 26 Redox-active (By similarity). SQ SEQUENCE 99 AA; 11344 MW; 2037C6E75986C413 CRC64; MEKFEDLIQS PIPVLVDFFA EWCGPCKAMK PVLEELKTMV GDKARIVKID VDQHEDLATK YRIQAVPTFI LFKNGEAVWR HSGVIHSSEL KGIIEQNYI //