ID R7T6A1_CAPTE Unreviewed; 100 AA.
AC R7T6A1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glutaredoxin-1 {ECO:0000256|ARBA:ARBA00013662};
GN ORFNames=CAPTEDRAFT_162446 {ECO:0000313|EMBL:ELT88955.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT88955.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELT88955.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT88955.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP162446}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00002549}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {ECO:0000256|ARBA:ARBA00007787}.
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DR EMBL; AMQN01015099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMQN01015100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB311595; ELT88955.1; -; Genomic_DNA.
DR AlphaFoldDB; R7T6A1; -.
DR STRING; 283909.R7T6A1; -.
DR EnsemblMetazoa; CapteT162446; CapteP162446; CapteG162446.
DR HOGENOM; CLU_026126_7_2_1; -.
DR OMA; EYACYEL; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR047185; GLRX1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR46185; GLUTAREDOXIN-1; 1.
DR PANTHER; PTHR46185:SF1; GLUTAREDOXIN-1; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000014760}.
FT DOMAIN 19..85
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 100 AA; 11549 MW; A0830EB70DADEE34 CRC64;
MVNQEVKTLV DGKIAGKKVM IFSKTHCPYC VKAKDVMKKH FGKDLKEEDY EVLEIENLPE
CQEIQDYLKT LTGARSVPRV FINGRCREER TAFQTARLNV
//
