PTC71_DROER
ID PTC71_DROER Reviewed; 317 AA.
AC B3P5D3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=GG12003;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV53183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV53183.1};
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; CH954182; EDV53183.1; -; Genomic_DNA.
DR RefSeq; XP_001981313.1; XM_001981277.2.
DR AlphaFoldDB; B3P5D3; -.
DR SMR; B3P5D3; -.
DR STRING; 7220.FBpp0130549; -.
DR PRIDE; B3P5D3; -.
DR EnsemblMetazoa; FBtr0132057; FBpp0130549; FBgn0104295.
DR GeneID; 6554553; -.
DR KEGG; der:6554553; -.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_3_0_1; -.
DR OMA; DSWFVSS; -.
DR OrthoDB; 826926at2759; -.
DR PhylomeDB; B3P5D3; -.
DR Proteomes; UP000008711; 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 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.
FT CHAIN 1..317
FT /note="Protein phosphatase PTC7 homolog fig"
FT /id="PRO_0000377396"
FT DOMAIN 46..312
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 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
SQ SEQUENCE 317 AA; 35294 MW; 4894B4356ADDB560 CRC64;
MITRLKNWPR LLKTPLQIAR HSIQQFSHLA GHYERPPQSG KSSRDPYLVT VVQGRSKKPR
FPGERANQRF GEDSWFVRST PLAEVMGVAD GVGGWRDVGV DAGRFAKELM TCCSGQTQRS
GFDGRSPRNL LIASFQELTH REHPVVGSST ACLATMHRKD CTLYTANLGD SGFLVVRNGR
VLHRSVEQTH DFNTPYQLTV PPEDRKECYY CDKPEMAVST RHSLLPGDLV LLATDGLFDN
MPESMLLKIL NGLKERGERD LLQCASQVVE KARELSLNAT FQSPFAIKAR QHNVSYSGGG
KPDDITLILA SVEVQSA
