ID   GLRX_ENCCU              Reviewed;         129 AA.
AC   Q8SUM8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glutaredoxin-like protein ECU08_1380;
GN   OrderedLocusNames=ECU08_1380;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC   -!- CAUTION: May be inactive since it lacks one cysteine involved the
CC       redox-active disulfide bond. {ECO:0000305}.
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DR   EMBL; AL590448; CAD26442.2; -; Genomic_DNA.
DR   RefSeq; NP_597266.1; NM_001041875.1.
DR   AlphaFoldDB; Q8SUM8; -.
DR   SMR; Q8SUM8; -.
DR   STRING; 284813.Q8SUM8; -.
DR   GeneID; 859688; -.
DR   KEGG; ecu:ECU08_1380; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1380; -.
DR   HOGENOM; CLU_2061463_0_0_1; -.
DR   InParanoid; Q8SUM8; -.
DR   OrthoDB; 1596425at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Electron transport; Redox-active center; Reference proteome;
KW   Transport.
FT   CHAIN           1..129
FT                   /note="Glutaredoxin-like protein ECU08_1380"
FT                   /id="PRO_0000383029"
FT   DOMAIN          26..126
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
SQ   SEQUENCE   129 AA;  14465 MW;  05544D3711E433A5 CRC64;
     MKAVLLALAL VYGSQGTEYG GGKMTEADYG EMVRREKCIM FVKRFCPYSI RARELLHDRG
     VGCKIIEVDN NLDAYSFAKR NHSTFPVFFL DGDLVEGGCE KLLVLSDSNL PPFDKSPLLT
     QNREPVLLD