ID B3NBS5_DROER Unreviewed; 241 AA. AC B3NBS5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV50671.1}; DE EC=2.5.1.18 {ECO:0000313|EMBL:EDV50671.1}; GN Name=Dere\GG14320 {ECO:0000313|EMBL:EDV50671.1}; GN ORFNames=Dere_GG14320 {ECO:0000313|EMBL:EDV50671.1}; OS Drosophila erecta (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7220 {ECO:0000313|EMBL:EDV50671.1}; RN [1] {ECO:0000313|EMBL:EDV50671.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV50671.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDV50671.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV50671.1}; RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542; RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.; RT "Assembly reconciliation."; RL Bioinformatics 24:42-45(2008). RN [3] {ECO:0000313|EMBL:EDV50671.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV50671.1}; RG FlyBase; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family. CC {ECO:0000256|ARBA:ARBA00011067}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH954178; EDV50671.1; -; Genomic_DNA. DR RefSeq; XP_001971645.1; XM_001971609.2. DR AlphaFoldDB; B3NBS5; -. DR EnsemblMetazoa; FBtr0134374; FBpp0132866; FBgn0106581. DR GeneID; 6545778; -. DR KEGG; der:6545778; -. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_9_2_1; -. DR OMA; FGACFCP; -. DR OrthoDB; 103277at2759; -. DR PhylomeDB; B3NBS5; -. DR Proteomes; UP000008711; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:EnsemblMetazoa. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0006749; P:glutathione metabolic process; IEA:EnsemblMetazoa. DR CDD; cd03184; GST_C_Omega; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR005442; GST_omega. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43968; -; 1. DR PANTHER; PTHR43968:SF6; GLUTATHIONE S-TRANSFERASE OMEGA; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF13417; GST_N_3; 1. DR PRINTS; PR01625; GSTRNSFRASEO. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Transferase {ECO:0000313|EMBL:EDV50671.1}. FT DOMAIN 20..102 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 107..226 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 241 AA; 27811 MW; C6E06CEDCA033C96 CRC64; MSSGKHLTKG SPKPALPDDG VLRLYSMRFC PYAQRAHLVL NAKNVPHHSI YINLTEKPEW LVDVSPLLKV PALQLVAEKD QPSLIESLII AEYLDEKYPE NPLLPKDPLR RAQDKILLER FSGITNAFMK ILLQSTGLED YWAALDIFEQ ELTKRGTPYF GGNKPGFVDY MIWPWFERLS VIELKLQEEY NFDEARFPKI SKWIALLKAD SVVKSFYATP EQHNEFWRTR KAGNANYDLL A //