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Database: UniProt
Entry: I1GWC4_BRADI
LinkDB: I1GWC4_BRADI
Original site: I1GWC4_BRADI 
ID   I1GWC4_BRADI            Unreviewed;       314 AA.
AC   I1GWC4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   Name=100825080 {ECO:0000313|EnsemblPlants:KQK17237};
GN   ORFNames=BRADI_1g33190v3 {ECO:0000313|EMBL:KQK17237.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK17237.1};
RN   [1] {ECO:0000313|EMBL:KQK17237.1, ECO:0000313|EnsemblPlants:KQK17237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK17237.1,
RC   ECO:0000313|EnsemblPlants:KQK17237};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK17237.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK17237.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK17237}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK17237};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CM000880; KQK17237.1; -; Genomic_DNA.
DR   RefSeq; XP_003563446.1; XM_003563398.3.
DR   AlphaFoldDB; I1GWC4; -.
DR   STRING; 15368.I1GWC4; -.
DR   EnsemblPlants; KQK17237; KQK17237; BRADI_1g33190v3.
DR   GeneID; 100825080; -.
DR   Gramene; KQK17237; KQK17237; BRADI_1g33190v3.
DR   KEGG; bdi:100825080; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   HOGENOM; CLU_050131_0_0_1; -.
DR   InParanoid; I1GWC4; -.
DR   OMA; IVAHMRP; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000008810; Chromosome 1.
DR   ExpressionAtlas; I1GWC4; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR   GO; GO:0005507; F:copper ion binding; IEA:EnsemblPlants.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          147..310
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          77..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         189
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         274
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        185..189
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   314 AA;  33763 MW;  14819E66464F5538 CRC64;
     MMKRHALQLL ARAVPHTSAP PAPPARFRPQ VAALKGWGSR GASAGFFSTD AAAATPAAPG
     AAQGGAKPAA AVAATVSGGG GEGGGQDGKS GQGGAGKSVR GGPVSWLSFL LLLVTGGGII
     VYYDKEKKRH IEELKNKTNS VKPGQSVGTA AIGGPFTLLN HDGKPVTEKD FLGKWTLLYF
     GFTHCPDICP DELQKMAAAI DKIKERTKIE IVPVFISVDP ERDTVEQVHD YVKEFHKDLI
     GLTGTTDEVR QVARAYRVYY MKTEEEGSDY LVDHSIVMYL MNPKMEFVKF FGKNYDVDSL
     AEGIVKEIRE HKSS
//
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