ID   PTC71_DROWI             Reviewed;         315 AA.
AC   B4NBL6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=GK19179;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1] {ECO:0000312|EMBL:EDW81180.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW81180.1};
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; CH964232; EDW81180.1; -; Genomic_DNA.
DR   RefSeq; XP_002070194.2; XM_002070158.2.
DR   AlphaFoldDB; B4NBL6; -.
DR   SMR; B4NBL6; -.
DR   STRING; 7260.B4NBL6; -.
DR   EnsemblMetazoa; FBtr0249830; FBpp0248322; FBgn0221177.
DR   GeneID; 6647958; -.
DR   KEGG; dwi:6647958; -.
DR   eggNOG; KOG1379; Eukaryota.
DR   HOGENOM; CLU_029404_3_0_1; -.
DR   OMA; DSWFVSS; -.
DR   OrthoDB; 240602at2759; -.
DR   PhylomeDB; B4NBL6; -.
DR   Proteomes; UP000007798; 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; PF13672; PP2C_2; 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..315
FT                   /note="Protein phosphatase PTC7 homolog fig"
FT                   /id="PRO_0000377405"
FT   DOMAIN          54..309
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         86
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         86
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
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         231
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   315 AA;  34550 MW;  C106A5802B5C9AAA CRC64;
     MLSSLAGKLQ GKTKFLIDVL KFYDARMLKS SSMSGIGKRG DPYLVKVVQG RSRKHSIASA
     KDNHRYGEDS WFISSTPKAE VMGVADGVGG WSELGIDSGL FASELMFWCA NYAKRESFDG
     RTPLDLLIES YSEIKGKTDP IVGSSTACLV SLNRRDCTMH SANLGDSGFL VIRNGRMLHR
     SEEQVHDFNA PYQLTVVPNE RFDNVYCDRP ELADSTRLPL QEGDLVLLAT DGLFDNVPES
     LIVKTLGKYQ GVTREEDLQS AANSLVHMAK DLSISPNFES PFALKAKAFE VDYPGGGKPD
     DITVILATVA VPQND
//