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Database: UniProt
Entry: D6WWF8_TRICA
LinkDB: D6WWF8_TRICA
Original site: D6WWF8_TRICA 
ID   D6WWF8_TRICA            Unreviewed;       379 AA.
AC   D6WWF8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFA08711.2};
GN   Name=AUGUSTUS-3.0.2_06382 {ECO:0000313|EMBL:EFA08711.2};
GN   ORFNames=TcasGA2_TC006382 {ECO:0000313|EMBL:EFA08711.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA08711.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA08711.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08711.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA08711.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08711.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
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DR   EMBL; KQ971361; EFA08711.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6WWF8; -.
DR   STRING; 7070.D6WWF8; -.
DR   EnsemblMetazoa; TC006382_001; TC006382_001; TC006382.
DR   HOGENOM; CLU_837665_0_0_1; -.
DR   InParanoid; D6WWF8; -.
DR   Proteomes; UP000007266; Linkage group 8.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR024336; tRNA_splic_suSen54_N.
DR   NCBIfam; TIGR02180; GRX_euk; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   PANTHER; PTHR45694:SF30; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   Pfam; PF12928; tRNA_int_end_N2; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          50..115
FT                   /note="tRNA-splicing endonuclease subunit Sen54 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12928"
FT   DOMAIN          297..358
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   379 AA;  42734 MW;  FC379197575237B3 CRC64;
     MSLKDTVEKY FHDHNNPVVK TESFGAKLFL SPLSDDEEGR KNRCLSGIET VLRHTRVERR
     VARSVAEWLP NRNVAQVTKV TGSLKGGFGA QTKDGKILSP EETLFLLEAN KIELRLDKVP
     LSIQEAYKTI QLNHAKYHAY KKLVLQGFKV KPLTTINQEE TTKRKLESDD GPSAKVAKTN
     DEQMAPIFEK LREMGPQPFN GQGHHSTADY TVKSSTNSDC FNLVFKSSDE FTSIDPNQPD
     STLYSVCSDD NVAFYNFSRA YLIFQRQIKH LEHSKLPIDM SSPKVEVVKD LIKSDTVVIF
     SKTYCPYCKL AKEVFNNLKK TFTTIELDKR DDGEEIQGIL GELTGAKTVP RVFVKGQCLG
     GGSDVKALYD KGELQKYFD
//
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