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PTC71_DROGR
ID   PTC71_DROGR             Reviewed;         307 AA.
AC   B4JYN1;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, 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=GH13984;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1] {ECO:0000312|EMBL:EDV90793.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV90793.1};
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; CH916377; EDV90793.1; -; Genomic_DNA.
DR   RefSeq; XP_001996135.1; XM_001996099.1.
DR   AlphaFoldDB; B4JYN1; -.
DR   SMR; B4JYN1; -.
DR   STRING; 7222.FBpp0147890; -.
DR   EnsemblMetazoa; FBtr0149398; FBpp0147890; FBgn0121460.
DR   GeneID; 6569641; -.
DR   KEGG; dgr:6569641; -.
DR   eggNOG; KOG1379; Eukaryota.
DR   HOGENOM; CLU_029404_3_0_1; -.
DR   InParanoid; B4JYN1; -.
DR   OMA; DSWFVSS; -.
DR   OrthoDB; 826926at2759; -.
DR   PhylomeDB; B4JYN1; -.
DR   Proteomes; UP000001070; 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;
KW   Reference proteome.
FT   CHAIN           1..307
FT                   /note="Protein phosphatase PTC7 homolog fig"
FT                   /id="PRO_0000377397"
FT   DOMAIN          41..300
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   307 AA;  33875 MW;  1D17E6A3C5762800 CRC64;
     MFFKVCQLGK GRCCQVLLNY ASCQRCQLSS YKGTPRLIKA VQGSSKDQQL AGQVQRFGED
     SWFVHSAPKS ETMGVADGVG GWRQMGIDSG VFAKQLMTNC SKLSEQADYD GRNPRQLLID
     GYHRLKEHAT NVWGSSTACL VSLHRSDCTL HSANLGDSGF LVLRHGKVLH RSDEQLHVFN
     TPYQLSVPPT SQMHKVLSDQ PEEAICTQLG LQQGDLVLVA TDGLFDNVVE SELVQQLQQL
     HGETRVEKVQ LAANRLVDLA KRLSLRTDYQ SPFALRAKAN NMNYGAGGKP DDITVILASV
     EVSQRSN
 
 
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