ID Q011R3_OSTTA Unreviewed; 340 AA.
AC Q011R3;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Thioredoxin, conserved site {ECO:0000313|EMBL:CAL55367.1};
GN ORFNames=OT_ostta09g02110 {ECO:0000313|EMBL:CAL55367.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CAL55367.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000256|ARBA:ARBA00008983}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAL55367.1}.
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DR EMBL; CAID01000009; CAL55367.1; -; Genomic_DNA.
DR RefSeq; XP_003081198.1; XM_003081150.1.
DR AlphaFoldDB; Q011R3; -.
DR STRING; 70448.Q011R3; -.
DR GeneID; 9831776; -.
DR KEGG; ota:OT_ostta09g02110; -.
DR InParanoid; Q011R3; -.
DR OMA; CEPCTAV; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000009170; Chromosome 9.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 2.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 2.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 1..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 340 AA; 36696 MW; CB11E647C7FCA378 CRC64;
MSVALTDAVA YDAFTAARDR AIVHFTASWC EPCAAMEIVL EKIREKHAGV VTATCDAEAV
EDVAEREGVS AVPYFVFYRD GKRVDAVEGA DAATVTNKTR MYFPATATQT TATTAKGADA
VKSTEASGKQ ALQARLKSLI ESQPVVLFMK GHPDEPKCGF SRKVVDALNG AGIKFGSFNI
LADEDVRQGL KEYSNWPTYP QLYVDGELLG GCDIILEMAE SGELAEACSE ASGDGKVKKA
LNERIKRMLD AQDVILFMKG DRNVPRCGFS GKVVKALDAT GVEYATFDIL GDEPIRQGLK
EYSNWPTYPQ LYYKGELIGG CDIILELAEA GELATELGAA
//
