ID A0A061DFF0_THECC Unreviewed; 130 AA.
AC A0A061DFF0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glutaredoxin-1, grx1, putative {ECO:0000313|EMBL:EOX90939.1};
GN ORFNames=TCM_000270 {ECO:0000313|EMBL:EOX90939.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX90939.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX90939.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC {ECO:0000256|ARBA:ARBA00007190}.
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DR EMBL; CM001879; EOX90939.1; -; Genomic_DNA.
DR RefSeq; XP_007046782.1; XM_007046720.2.
DR AlphaFoldDB; A0A061DFF0; -.
DR SMR; A0A061DFF0; -.
DR STRING; 3641.A0A061DFF0; -.
DR EnsemblPlants; EOX90939; EOX90939; TCM_000270.
DR EnsemblPlants; Tc01v2_t002140.1; Tc01v2_p002140.1; Tc01v2_g002140.
DR GeneID; 18610828; -.
DR Gramene; EOX90939; EOX90939; TCM_000270.
DR Gramene; Tc01v2_t002140.1; Tc01v2_p002140.1; Tc01v2_g002140.
DR KEGG; tcc:18610828; -.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; A0A061DFF0; -.
DR OMA; EYACYEL; -.
DR OrthoDB; 903at2759; -.
DR Proteomes; UP000026915; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR PANTHER; PTHR45694:SF4; GLUTAREDOXIN-C3; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..130
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001600329"
FT DOMAIN 46..108
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 130 AA; 14348 MW; DFED57FD414E8331 CRC64;
MTRSRFILTI FGTVVVLLLA GNALRQAKAN NSASAFVQNT IFSHKIVIFS KSYCPYCFRA
KRIFSELSEK PYVVELDLRD DGGKIQYVLL DLVGRSTVPQ VFVKGKHIGG SDDLKDAVHS
GKLQKLLAAS
//
