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Database: UniProt
Entry: D8SFT3_SELML
LinkDB: D8SFT3_SELML
Original site: D8SFT3_SELML 
ID   D8SFT3_SELML            Unreviewed;       410 AA.
AC   D8SFT3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
DE   Flags: Fragment;
GN   ORFNames=SELMODRAFT_115826 {ECO:0000313|EMBL:EFJ16782.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ16782.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000696};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001346};
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DR   EMBL; GL377617; EFJ16782.1; -; Genomic_DNA.
DR   RefSeq; XP_002982114.1; XM_002982068.1.
DR   AlphaFoldDB; D8SFT3; -.
DR   EnsemblPlants; EFJ16782; EFJ16782; SELMODRAFT_115826.
DR   Gramene; EFJ16782; EFJ16782; SELMODRAFT_115826.
DR   KEGG; smo:SELMODRAFT_115826; -.
DR   eggNOG; KOG2501; Eukaryota.
DR   HOGENOM; CLU_019626_0_2_1; -.
DR   InParanoid; D8SFT3; -.
DR   OMA; ENTTLIW; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR004146; DC1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13871:SF103; CN HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13871; THIOREDOXIN; 1.
DR   Pfam; PF03107; C1_2; 1.
DR   Pfam; PF13905; Thioredoxin_8; 2.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN          13..113
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13905"
FT   DOMAIN          185..280
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13905"
FT   DOMAIN          327..373
FT                   /note="DC1"
FT                   /evidence="ECO:0000259|Pfam:PF03107"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFJ16782.1"
SQ   SEQUENCE   410 AA;  46667 MW;  3FE208E87E3C9FF3 CRC64;
     PSLGKVETKV LEGKIVGLLF SVESNKSCSN FVNKLLGIYD EIQKISTAGA GGVGFEVVFV
     SGDTDEASFK QSMKKMPWLA LPFDVKGATT AKLARRFKVE VMPSLVLVGS NGTTLLSRYG
     YSLVTRFGSK AFPFTQEHIR DLEKVEDQNA SKLPVELKDG AHEHRDYVIR NDGSKVSIQS
     LQGFKCYGLA FVAHWYPTAR AFVDKHLIPL YEQIRARHGK RSIEIIFVSD DVNYIEFMEF
     FQTMPWLALP FQDRRTELIL STKLNVQSIP AFAIFDGDGK LLFREGRSVI LRHGSRAYPF
     TPHHVSKLDV IQRKRASKLP ADVKHPQHEH TLDLVRDWYD NFGMFVCDAC LDEGNGWFYH
     CERCSWDLHP ACANPKFDLQ KSGSTDFRCY CYRANIFKKM LKLQPKETLT
//
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