ID A0A3P6S8X0_LITSI Unreviewed; 589 AA.
AC A0A3P6S8X0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=NLS_LOCUS475 {ECO:0000313|EMBL:VDK68607.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK68607.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK68607.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; UYRX01000012; VDK68607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6S8X0; -.
DR STRING; 42156.A0A3P6S8X0; -.
DR Proteomes; UP000277928; 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; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
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; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 2.
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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928}.
FT DOMAIN 23..573
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 213..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 65158 MW; 57EB87DC3EED721C CRC64;
MGAYLNKPIT EKVSECGGND RISYAATSMQ GWRINQEDAH NCIVNYDGDS SFFAVYDGHG
GSEVARYSAH HLPDMLKRNN SWFSGNYVKA MQDTFLELDE LLRTEAVMKE LKRIAGSVEP
KHEELSDDDE DKQTLYEEAG MPIETILERY GIVLHREQNG KQSIIDLNEL RTQLEQQGGG
EEQVQKMEQF EKKIQENGLN VLEQERNWKD QNGDAVIDKE VKARKNQLRK TEEKAVEGRT
KKRMSELSPS LLRAKRTKSS NDIEEGTLES QSNDTSPSRS AVDKSEERIQ DERCETAEIA
GESEEANSEP EVAGTAEIST TTQSIDSGDT DECAPPGKNP HPSATSDGQI TFSSDSESVD
EDYNADEEMS EGEEEEEMDD EEIDAEQAYS CPSGDTPGED SGTTACVVVV FKDKVVVSNA
GDSRAVMCRN GVAVELSIDH KPEDDIERRR IETAGGEISM DGRVNGGLNL SRALGDHFYK
KNASLPLKEQ MISALPDVKQ YKILQDDEFI IIACDGIWNS LTSQEAVDFV RRKINDGVSL
KDICEQVCDH CLSPNTAGDG TGCDNMTIII VQILRSASLS QKLATPSSS
//
