GenomeNet

Database: UniProt
Entry: B3EJM4_CHLPB
LinkDB: B3EJM4_CHLPB
Original site: B3EJM4_CHLPB 
ID   B3EJM4_CHLPB            Unreviewed;       268 AA.
AC   B3EJM4;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:ACE04393.1};
GN   OrderedLocusNames=Cphamn1_1467 {ECO:0000313|EMBL:ACE04393.1};
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE04393.1};
RN   [1] {ECO:0000313|EMBL:ACE04393.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1 {ECO:0000313|EMBL:ACE04393.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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; CP001101; ACE04393.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3EJM4; -.
DR   STRING; 331678.Cphamn1_1467; -.
DR   KEGG; cpb:Cphamn1_1467; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_046120_1_1_10; -.
DR   OrthoDB; 9790390at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14561; TPR_20; 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          1..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   268 AA;  30302 MW;  C684D1B2823AAE39 CRC64;
     MQDRAFDFGR DVQERSNEIP VLVDFWAEWC GPCRMLGPVL EKVTEHHAGE FVLVKVNTEE
     HPDIAREYGI MSIPAVKLFI RGEVADEFVG AMTERQVEDW LKKALPGKYA DQLLEALSFV
     TQGKEDAATS ILEMILKNEP ANKEAAAVLL KLTIFSAPEA AVAMIDGLEG EYAYAELVAS
     ARTITGLLLL DTAPLPDDPV KDRYLSAIEH MRRKEFDSAL VRFIEVIRQN RYYDDDSARK
     ACIAIFKYLG EDDPTTLKHR RSFDRALY
//
DBGET integrated database retrieval system