(data stored in ACNUC5340 zone)

SWISSPROT: C3PMP6_RICAE

ID   C3PMP6_RICAE            Unreviewed;       102 AA.
AC   C3PMP6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   Name=grxC1 {ECO:0000313|EMBL:ACP53206.1};
GN   OrderedLocusNames=RAF_ORF0249 {ECO:0000313|EMBL:ACP53206.1};
OS   Rickettsia africae (strain ESF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=347255 {ECO:0000313|EMBL:ACP53206.1, ECO:0000313|Proteomes:UP000002305};
RN   [1] {ECO:0000313|EMBL:ACP53206.1, ECO:0000313|Proteomes:UP000002305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESF-5 {ECO:0000313|EMBL:ACP53206.1,
RC   ECO:0000313|Proteomes:UP000002305};
RX   PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA   Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA   Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT   "Analysis of the Rickettsia africae genome reveals that virulence
RT   acquisition in Rickettsia species may be explained by genome
RT   reduction.";
RL   BMC Genomics 10:166-166(2009).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
CC       the presence of NADPH and glutathione reductase. Reduces low
CC       molecular weight disulfides and proteins.
CC       {ECO:0000256|RuleBase:RU364065}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|RuleBase:RU364065}.
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DR   EMBL; CP001612; ACP53206.1; -; Genomic_DNA.
DR   RefSeq; WP_012719469.1; NC_012633.1.
DR   EnsemblBacteria; ACP53206; ACP53206; RAF_ORF0249.
DR   KEGG; raf:RAF_ORF0249; -.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; GRTTFPQ; -.
DR   BioCyc; RAFR347255:G1GVG-433-MONOMER; -.
DR   Proteomes; UP000002305; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02181; GRX_bact; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3PMP6.
DR   SWISS-2DPAGE; C3PMP6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002305};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW   Electron transport {ECO:0000256|RuleBase:RU364065};
KW   Redox-active center {ECO:0000256|RuleBase:RU364065};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN        1     96       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
SQ   SEQUENCE   102 AA;  11375 MW;  696B66C13483CA97 CRC64;
     MNKAILHTII VYTLSSCPYC IKAKALLDEK NVAYEEIEVS NFTREEKEKF IKKSGGKKTV
     PQIFIDNMHV GGCDALFDLE KEGRLDKLLE NQPKTTSPAA GA
//

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