(data stored in ACNUC5340 zone)

SWISSPROT: Q5FG21_EHRRG

ID   Q5FG21_EHRRG            Unreviewed;       110 AA.
AC   Q5FG21;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   Name=grxC2 {ECO:0000313|EMBL:CAI28172.1};
GN   OrderedLocusNames=ERGA_CDS_07200 {ECO:0000313|EMBL:CAI28172.1};
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI28172.1, ECO:0000313|Proteomes:UP000000533};
RN   [1] {ECO:0000313|EMBL:CAI28172.1, ECO:0000313|Proteomes:UP000000533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel {ECO:0000313|EMBL:CAI28172.1,
RC   ECO:0000313|Proteomes:UP000000533};
RX   PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J.,
RA   Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia
RT   ruminantium reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
CC       subfamily. {ECO:0000256|PIRNR:PIRNR005894}.
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DR   EMBL; CR925677; CAI28172.1; -; Genomic_DNA.
DR   RefSeq; WP_011255796.1; NC_006831.1.
DR   EnsemblBacteria; CAI28172; CAI28172; ERGA_CDS_07200.
DR   KEGG; erg:ERGA_CDS_07200; -.
DR   HOGENOM; HOG000095211; -.
DR   KO; K07390; -.
DR   OMA; KGTKLMP; -.
DR   OrthoDB; 2001991at2; -.
DR   BioCyc; ERUM302409:ERGA_RS03685-MONOMER; -.
DR   Proteomes; UP000000533; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; 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   CDD; cd03028; GRX_PICOT_like; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR014434; Monothiol_GRX.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR10293; PTHR10293; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00365; TIGR00365; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5FG21.
DR   SWISS-2DPAGE; Q5FG21.
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000533};
KW   Iron {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR005894-2}.
FT   DOMAIN        6    108       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   METAL        31     31       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000256|PIRSR:PIRSR005894-
FT                                2}.
SQ   SEQUENCE   110 AA;  12614 MW;  5E0800B82A707ED9 CRC64;
     MTNNIMNRIK HDIETNDVVL YMKGDANMPQ CGFSSVVVTI LKKMNISFKS INVLEDQELR
     EAIKEFTNWP TIPQLYVKGE FIGGCDIVKE MYHTGELQEL FVKNNLITAN
//

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