ID   PTC71_DROMO             Reviewed;         312 AA.
AC   B4K616;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=GI22329;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1] {ECO:0000312|EMBL:EDW16253.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW16253.1};
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}.
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DR   EMBL; CH933806; EDW16253.1; -; Genomic_DNA.
DR   RefSeq; XP_002000792.1; XM_002000756.2.
DR   AlphaFoldDB; B4K616; -.
DR   SMR; B4K616; -.
DR   EnsemblMetazoa; FBtr0173054; FBpp0171546; FBgn0145057.
DR   KEGG; dmo:Dmoj_GI22329; -.
DR   eggNOG; KOG1379; Eukaryota.
DR   HOGENOM; CLU_029404_3_0_1; -.
DR   InParanoid; B4K616; -.
DR   OMA; DSWFVSS; -.
DR   OrthoDB; 5399209at2759; -.
DR   PhylomeDB; B4K616; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
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..312
FT                   /note="Protein phosphatase PTC7 homolog fig"
FT                   /id="PRO_0000377399"
FT   DOMAIN          42..306
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         84
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         228
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   312 AA;  34487 MW;  307F370C8726CDED CRC64;
     MFFTVRNLSN RTSQVVNYAY IQYRLLSSTT KTKGLPRLIK AIQGSSKDQL ADDHLHMIDD
     HRYGEDSWFV SSTPKAETMG VADGVGGWRR LGIDSGLFAQ ELMTNCSEFA EQPQYDGSDP
     RQLLIDSFDQ MKKMSGKVCG SSTACLVTLH RRDCTLHSAN LGDSGFMVLR NGKVLHRSDE
     QLHGFNTPYQ LTVAPEPGMD CILCDSPQQA VTSHINVQQG DLVLLATDGL FDNVPESMLV
     RHLQPLHGET RMEHLQHAVN RLVDMAKTLS LSNTFQSPFA LKAKASNMNY GVGGKPDDIT
     VILASVDVPD KD
//