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PTC71_DROPS
ID   PTC71_DROPS             Reviewed;         340 AA.
AC   Q29AP0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein phosphatase PTC7 homolog fig;
DE   AltName: Full=Fos intronic gene protein;
DE            EC=3.1.3.16;
GN   Name=fig {ECO:0000250|UniProtKB:Q9VAH4}; ORFNames=GA20482;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL27309.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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;
CC         Evidence={ECO:0000250|UniProtKB:P35813, ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P35813, ECO:0000305};
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000255}.
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DR   EMBL; CM000070; EAL27309.2; -; Genomic_DNA.
DR   RefSeq; XP_001358172.2; XM_001358135.3.
DR   AlphaFoldDB; Q29AP0; -.
DR   SMR; Q29AP0; -.
DR   STRING; 7237.FBpp0283509; -.
DR   PRIDE; Q29AP0; -.
DR   EnsemblMetazoa; FBtr0285071; FBpp0283509; FBgn0080477.
DR   GeneID; 4800997; -.
DR   KEGG; dpo:Dpse_GA20482; -.
DR   eggNOG; KOG1379; Eukaryota.
DR   HOGENOM; CLU_029404_3_0_1; -.
DR   InParanoid; Q29AP0; -.
DR   OMA; DSWFVSS; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0080477; Expressed in male reproductive system and 1 other tissue.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:EnsemblMetazoa.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   InterPro; IPR039123; PPTC7.
DR   PANTHER; PTHR12320; PTHR12320; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..340
FT                   /note="Protein phosphatase PTC7 homolog fig"
FT                   /id="PRO_0000377401"
FT   DOMAIN          58..314
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   340 AA;  37443 MW;  280EE1765CA1AABA CRC64;
     MAFMRSKPSL GSLARVAFRW CGPGVGLVNY SQEPYLVKAV QGKSKPRSPT LQSAMQPRAQ
     AETIQAPKCF GEDSFFFSST PKADVMGVAD GVGGWRDRGI DAGRFSRDLM QRCFVHAQKP
     TFDGRNPRQL LSECYGEMKR KWKPILGSST ACVVAFNRSE SALYTANLGD SGYVVIRNGS
     VLDRSEEQTH FFNMPFQLTV PPPDSNREMW FCDDPSEAVA TRLLLQPDDL VLVATDGLFD
     NMPEQMLLEM LSKVQGVHEQ KAIQEAVNRV VERAGALSIN PIYKSPFCLR ALENNVAYGG
     GGKPDDITVV LASVAMRQCN TVGDSNESKG SDLRPRLSFP
 
 
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