PTC71_DROYA
ID PTC71_DROYA Reviewed; 320 AA.
AC B4PPK3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GE10429;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW98253.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW98253.1};
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; CM000160; EDW98253.1; -; Genomic_DNA.
DR RefSeq; XP_002098541.1; XM_002098505.2.
DR AlphaFoldDB; B4PPK3; -.
DR SMR; B4PPK3; -.
DR STRING; 7245.FBpp0255439; -.
DR EnsemblMetazoa; FBtr0256947; FBpp0255439; FBgn0228292.
DR GeneID; 6538006; -.
DR KEGG; dya:Dyak_GE10429; -.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_3_0_1; -.
DR OMA; DSWFVSS; -.
DR OrthoDB; 826926at2759; -.
DR PhylomeDB; B4PPK3; -.
DR Proteomes; UP000002282; 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 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..320
FT /note="Protein phosphatase PTC7 homolog fig"
FT /id="PRO_0000377406"
FT DOMAIN 49..315
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
SQ SEQUENCE 320 AA; 35522 MW; DB9C00AFF3F5EA3F CRC64;
MITHLKNWPR LLNRFVLQLK NARHSIHQFT HLAGRLQRPP KSGKSSRDPY LVTAVQGRSK
KPRYPGERAN QRFGEDSWFV SSTPLAEVMG VADGVGGWRD VGVDAGRFAK ELMTCCSGQT
QRSGFDGRSA RNLLIAGFQE LTHREQPVVG SSTACLATMH RRDCILYTAN LGDSGFLVVR
NGRVLHRSVE QTHDFNTPYQ LTVPPADRQD CYYCDKPEMA VSTRHSLLPG DLVLLATDGL
FDNMPESMLL KILNGLKERG ERDLLQGASQ VVEKARELSL NATFQSPFAI KARQHNVPYS
GGGKPDDITL ILASVEVPRA
