ID R0HAA9_9BRAS Unreviewed; 487 AA.
AC R0HAA9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=CARUB_v10000832mg {ECO:0000313|EMBL:EOA20518.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA20518.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000256|ARBA:ARBA00008983}.
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DR EMBL; KB870810; EOA20518.1; -; Genomic_DNA.
DR RefSeq; XP_006287620.1; XM_006287558.1.
DR AlphaFoldDB; R0HAA9; -.
DR STRING; 81985.R0HAA9; -.
DR GeneID; 17881496; -.
DR KEGG; crb:17881496; -.
DR eggNOG; KOG0911; Eukaryota.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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; 3.
DR CDD; cd02984; TRX_PICOT; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 3.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 3.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 3.
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:UP000029121}.
FT DOMAIN 1..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 487 AA; 53129 MW; 1753864A8563736E CRC64;
MSGTVKDMAS KAELDNLRQS GAPVVLHFWA SWCDASKQMD QVFSHLATDF PRAHFFRVEA
EEHPEISEAY SVAAVPYFVF FKDGKIVDTL EGADPSSLAN KVGKVAGSST SSEPAAPASL
GLAAGPTILE TVKENAKATV QDRAQPVSTA DALKNRLEKL TNSHPVMLFM KGVPEEPRCG
FSRKVVDILK DEKVEFGSFD ILSDNEVREG LKKFSNWPTF PQLYCNGELL GGADIAIAMH
ESGELKEAFK DLGITSVGSK ASQDEAVKGG VSSDNTGLSE TLRARLQGLV NSKPVMLFMK
GRPEEPKCGF SGKVVEILNQ EKIEFGSFDI LLDDEVRQGL KVYSNWSSYP QLYVKGELMG
GSDIVLEMQK SGELKKVLSE KGIAGKQSLE DRLKALINSS EVMLFMKGSP DEPQCGFSSK
VVKALRGENV SFGSFDILTD EEVRQGIKNF SNWPTFPQLY YKGELIGGCD IIMELSESGD
LKATLSE
//
