ID A0A267GTQ6_9PLAT Unreviewed; 397 AA.
AC A0A267GTQ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig015070g1 {ECO:0000313|EMBL:PAA89411.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA89411.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA89411.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA89411.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA89411.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA89411.1}.
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DR EMBL; NIVC01000151; PAA89411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GTQ6; -.
DR STRING; 282301.A0A267GTQ6; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF226; PROTEIN PHOSPHATASE 1K, MITOCHONDRIAL; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 114..368
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 17..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA89411.1"
SQ SEQUENCE 397 AA; 42927 MW; A1C2DC578B8C1035 CRC64;
QLAAALRQLA LLLPRRRLAG SSSSSSSAPA ATPAPAEPQR RPRRQSPAAA AAAASDAAAA
AVGAAPSPDG VRSTRLLTNS LMGLGSWKTR INYPILEQQS MRQGKLVPRI TCQYVGSCTS
QGRRQYQEDR LVYKDLQENL LFIGIFDGHG DAAAADFLVE RLPDLAHFWC RQQPRLDVAL
RRSFVEANNL FQRHLQRLSS GQAGRFASGS TATVCLLRNS TELAVANVGD SKAVLCRSGR
PELLSVDHDP ALEEEQARIH ARGGVVTSNS LGNPVVNGRL SMTRSIGDCE MKPFGVTAQP
HLRCLEVRHG RDAFLLLVTD GVAFVMSVKE MVDIASTCAT PQEAAEIIVD QAMQFGSEDN
TTAVILPFGS WGKYAKQMSC MPYSMGRNFL ANRFTSS
//
