(data stored in ACNUC7421 zone)

SWISSPROT: Q3IDJ0_PSEHT

ID   Q3IDJ0_PSEHT            Unreviewed;       108 AA.
AC   Q3IDJ0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 90.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   Name=trxA {ECO:0000313|EMBL:CAI85222.1};
GN   OrderedLocusNames=PSHAa0113 {ECO:0000313|EMBL:CAI85222.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85222.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85222.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; CR954246; CAI85222.1; -; Genomic_DNA.
DR   RefSeq; WP_011326840.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDJ0; -.
DR   STRING; 326442.PSHAa0113; -.
DR   EnsemblBacteria; CAI85222; CAI85222; PSHAa0113.
DR   GeneID; 32566638; -.
DR   KEGG; pha:PSHAa0113; -.
DR   eggNOG; ENOG4105K63; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OMA; DANQEFA; -.
DR   OrthoDB; POG091H03UW; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   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   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IDJ0.
DR   SWISS-2DPAGE; Q3IDJ0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Isomerase {ECO:0000313|EMBL:CAI85222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN        1    108       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     33     36       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000077-4}.
SQ   SEQUENCE   108 AA;  11865 MW;  D6FA8F56B7A1EDD3 CRC64;
     MSEKIIQITD DSFEADVLQS DKPVLVDFWA EWCGPCKMIA PILSEVAEEF DGRVTIAKLN
     IDQNAGTPPK FGIRGIPTLL LFKDGQVAAT KVGALSKTQL IEFLENNL
//

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