PTC71_DROVI
ID PTC71_DROVI Reviewed; 313 AA.
AC B4M5T5;
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=GJ10517;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW59011.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW59011.1};
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; CH940652; EDW59011.1; -; Genomic_DNA.
DR RefSeq; XP_002055899.2; XM_002055863.2.
DR AlphaFoldDB; B4M5T5; -.
DR SMR; B4M5T5; -.
DR STRING; 7244.FBpp0224934; -.
DR EnsemblMetazoa; FBtr0226442; FBpp0224934; FBgn0197797.
DR GeneID; 6632264; -.
DR KEGG; dvi:6632264; -.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_3_0_1; -.
DR InParanoid; B4M5T5; -.
DR OMA; DSWFVSS; -.
DR OrthoDB; 826926at2759; -.
DR PhylomeDB; B4M5T5; -.
DR Proteomes; UP000008792; 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; -; 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..313
FT /note="Protein phosphatase PTC7 homolog fig"
FT /id="PRO_0000377404"
FT DOMAIN 47..307
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 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
SQ SEQUENCE 313 AA; 34263 MW; F51FC723A8C3CCB7 CRC64;
MFFTVRTLSN RTSHVLNCAF AQCRLLSSTA SAKGVPRLIK AIQGSSKEPL TDLQLRLIGD
NRYGEDSWFV SSTPKAETMG VADGVGGWRK LGIDAGVFAR ELMSHCSEFA EQAEYDGLNP
RQLLIDSYDR LKNKRPCNVC GSSTACLVTL HRPDCTLHSA NLGDSGFLVL RNGRVLHRSD
EQLHCFNTPY QLTVPPHPAM DCVLRDSPEQ AVSTHLPLQP GDLVLLATDG LFDNVPESML
INQLRALQGE TRAEYLQQAA NRLVDLAKTL SVSPTFQSPF ALKARANNVD YGIGGKPDDI
TVILASLEVP DKL
