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Database: UniProt
Entry: D7SY28_VITVI
LinkDB: D7SY28_VITVI
Original site: D7SY28_VITVI 
ID   D7SY28_VITVI            Unreviewed;       302 AA.
AC   D7SY28;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   OrderedLocusNames=VIT_08s0105g00550 {ECO:0000313|EMBL:CBI22811.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI22811.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; FN595245; CBI22811.3; -; Genomic_DNA.
DR   RefSeq; XP_002263427.1; XM_002263391.3.
DR   AlphaFoldDB; D7SY28; -.
DR   STRING; 29760.D7SY28; -.
DR   PaxDb; 29760-VIT_08s0105g00550-t01; -.
DR   EnsemblPlants; Vitvi08g00675_t001; Vitvi08g00675_P001; Vitvi08g00675.
DR   GeneID; 100247202; -.
DR   Gramene; Vitvi08g00675_t001; Vitvi08g00675_P001; Vitvi08g00675.
DR   KEGG; vvi:100247202; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   HOGENOM; CLU_050131_0_0_1; -.
DR   InParanoid; D7SY28; -.
DR   OMA; IVAHMRP; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000009183; Chromosome 8.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          134..299
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          68..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         178
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         263
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        174..178
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   302 AA;  33738 MW;  957AB5B770B6F8FE CRC64;
     MANFASRSAQ LRYFRRYLCS RALNQCSSTQ PSPPLKFCNH FSSQSIMPLR PGIQTLMMHH
     RYLCGTAGKS DSGEGQKSDQ SSDAGKAVRG GPVSWLSFLL LIFTGAGLVF YYDNEKKRHI
     EEINASSTAV KEGPSAGKAA IGGPFNLIND EGKNVTEKDF FGKWTLIYFG FTHCPDICPD
     ELIKVADAVD KIKAKIGVDI VPVFISVDPE RDTVEQVHEY VKEFHPNLIG LTGNPDEVRK
     AARAYRVYYM KTEEEGSDYL VDHSIMMYLM GPKMDFVKNF GKNNDVDSLA NGIMEAMKKY
     KP
//
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