ID   PTC71_DROSI             Reviewed;         314 AA.
AC   B4R089;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=GD17671;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1] {ECO:0000312|EMBL:EDX14895.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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}.
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; CM000364; EDX14895.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4R089; -.
DR   SMR; B4R089; -.
DR   STRING; 7240.B4R089; -.
DR   HOGENOM; CLU_029404_3_0_1; -.
DR   OMA; DSWFVSS; -.
DR   PhylomeDB; B4R089; -.
DR   Proteomes; UP000000304; Chromosome 3r.
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   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR039123; PPTC7.
DR   PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 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..314
FT                   /note="Protein phosphatase PTC7 homolog fig"
FT                   /id="PRO_0000377403"
FT   DOMAIN          43..309
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         87
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         87
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         232
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   314 AA;  34834 MW;  8E662288B5A5052B CRC64;
     MITRMKNWPC LLKRFSIQQF HQFTHLSGRL ERAPQSGKSS RDPYLVTVVQ GRSKKPRFPG
     ERSNQRFGED SWFVSSTPLA EVMGVADGVG GWRDLGVDAG RFAKELMSCC SGQTQLSDFD
     GRSPRNLLIA GFQELSHREQ PVVGSSTACL ATMHRKDCTL YTANLGDSGF LVVRNGRVLH
     RSVEQTHDFN TPYQLTVPPE DRKESYYCDK PEMAVSTRHS LLPGDLVLLA TDGLFDNMPE
     STLLSILNGL KERGERDLLE GASRVVEKAR ELSLNASFQS PFAIKARQHN VSYSGGGKPD
     DITLILSSVE VPSV
//