ID Y0417_DROME Reviewed; 662 AA. AC Q7K4Q5; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 02-JUN-2021, entry version 119. DE RecName: Full=Probable protein phosphatase CG10417; DE EC=3.1.3.16; GN ORFNames=CG10417; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=17372656; DOI=10.1039/b617545g; RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., RA Eng J.K., Aebersold R., Tao W.A.; RT "An integrated chemical, mass spectrometric and computational strategy for RT (quantitative) phosphoproteomics: application to Drosophila melanogaster RT Kc167 cells."; RL Mol. Biosyst. 3:275-286(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-592; SER-594; RP SER-599; THR-637; SER-639 AND SER-641, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. 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; AE013599; AAF57333.1; -; Genomic_DNA. DR EMBL; AY051748; AAK93172.1; -; mRNA. DR RefSeq; NP_610169.1; NM_136325.3. DR RefSeq; NP_724410.1; NM_165430.2. DR SMR; Q7K4Q5; -. DR BioGRID; 61404; 2. DR IntAct; Q7K4Q5; 1. DR STRING; 7227.FBpp0085427; -. DR iPTMnet; Q7K4Q5; -. DR PaxDb; Q7K4Q5; -. DR PRIDE; Q7K4Q5; -. DR DNASU; 35492; -. DR EnsemblMetazoa; FBtr0086091; FBpp0085427; FBgn0033021. DR EnsemblMetazoa; FBtr0086092; FBpp0085428; FBgn0033021. DR GeneID; 35492; -. DR KEGG; dme:Dmel_CG10417; -. DR UCSC; CG10417-RA; d. melanogaster. DR FlyBase; FBgn0033021; CG10417. DR eggNOG; KOG0699; Eukaryota. DR GeneTree; ENSGT00940000172210; -. DR HOGENOM; CLU_013173_13_1_1; -. DR InParanoid; Q7K4Q5; -. DR OMA; CANMIEE; -. DR OrthoDB; 957254at2759; -. DR PhylomeDB; Q7K4Q5; -. DR BioGRID-ORCS; 35492; 0 hits in 3 CRISPR screens. DR ChiTaRS; CG10417; fly. DR GenomeRNAi; 35492; -. DR PRO; PR:Q7K4Q5; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0033021; Expressed in embryo and 40 other tissues. DR ExpressionAtlas; Q7K4Q5; baseline and differential. DR Genevisible; Q7K4Q5; DM. DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106306; F:protein serine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:FlyBase. DR GO; GO:0106307; F:protein threonine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; -; 2. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR PANTHER; PTHR13832; PTHR13832; 2. DR Pfam; PF00481; PP2C; 2. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; SSF81606; 2. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. PE 1: Evidence at protein level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT CHAIN 1..662 FT /note="Probable protein phosphatase CG10417" FT /id="PRO_0000372839" FT DOMAIN 23..564 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 219..275 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 288..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 591..662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..275 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 288..314 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..374 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 591..606 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..634 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 635..662 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 57 FT /note="Manganese 1" FT /evidence="ECO:0000250" FT METAL 57 FT /note="Manganese 2" FT /evidence="ECO:0000250" FT METAL 58 FT /note="Manganese 1; via carbonyl oxygen" FT /evidence="ECO:0000250" FT METAL 506 FT /note="Manganese 2" FT /evidence="ECO:0000250" FT METAL 555 FT /note="Manganese 2" FT /evidence="ECO:0000250" FT MOD_RES 289 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17372656" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 592 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 594 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 599 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 637 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 639 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" SQ SEQUENCE 662 AA; 72370 MW; C34171B9B030996E CRC64; MGAYLSHPKT DKTSTDQFNE LLAVGASSMQ GWRNSQEDAH NSILNFDNNT SFFAVYDGHG GAEVAQYCAD KLPHFLKNLE TYKNGQFEVA LKEAFLGFDK TLLDPSIVSI LKILAGEHNF VDAEADDYEE EDLAELQEES NLPLNEVLEK YKGLPQKKDL DLKSSDHKEN FKMRSPYFRG RRAAALAAEA TNKAVMDPSA KPDGSSTSAA AAAAALSADG VANSRNPSNV VNPMAGADSN TTTSINDLST KNAALKDDSV NDQNEGSNGT DFKHTLVSSS NKKLFATGSN DMTELNQSSK NEFTNSSTSK EFERNINSSQ DDEFTDDDAD YEENDNVKSP DTSSAESSDC TENDDDGDED GNEDSDEEET DEDQMANDNF CANMIEEPGK DSGCTAVVCL LQGRDLYVAN AGDSRCVISR SGQAIEMSID HKPEDDEEAS RIIKAGGRVT LDGRVNGGLN LSRALGDHAY KTNVTLPAEE QMISALPDIK KLIITPEDEF MVLACDGIWN YMSSEEVVEF VRCRLKDNKK LSTICEELFD NCLAPNTMGD GTGCDNMTAV IVQFKKKLQE LQSTIPPNQT EDKLLKTSEN VSHSLNDQSA SKRCASQNAD ADDEILEKNN SKRLKTDLEQ ENIKDRTPSP SNQNEDPTQK AIKEVTIIVS SS //