PTC71_DROWI
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 03-AUG-2022, entry version 71.
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.FBpp0248322; -.
DR EnsemblMetazoa; FBtr0249830; FBpp0248322; FBgn0221177.
DR GeneID; 6647958; -.
DR KEGG; dwi:6647958; -.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_3_0_1; -.
DR InParanoid; B4NBL6; -.
DR OMA; DSWFVSS; -.
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; -; 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..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