ID A0A1D3TIE4_9APIC Unreviewed; 854 AA.
AC A0A1D3TIE4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protein phosphatase PPM2, putative {ECO:0000313|EMBL:SCP04713.1};
GN Name=PPM2 {ECO:0000313|EMBL:SCP04713.1};
GN ORFNames=POCGH01_09045000 {ECO:0000313|EMBL:SCP04713.1};
OS Plasmodium ovale (malaria parasite P. ovale).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=36330 {ECO:0000313|EMBL:SCP04713.1, ECO:0000313|Proteomes:UP000242942};
RN [1] {ECO:0000313|EMBL:SCP04713.1, ECO:0000313|Proteomes:UP000242942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PocGH01 {ECO:0000313|EMBL:SCP04713.1};
RG Pathogen Informatics;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enzyme with a broad specificity.
CC {ECO:0000256|ARBA:ARBA00003302}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT594590; SCP04713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3TIE4; -.
DR VEuPathDB; PlasmoDB:PocGH01_09045000; -.
DR VEuPathDB; PlasmoDB:POWCR01_090040300; -.
DR Proteomes; UP000242942; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:UP000242942}.
FT DOMAIN 26..835
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 188..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96061 MW; DBEB9102C0A1F4CE CRC64;
MGAYLSAPKT NKESLDGGSL ELDPSRYGLS CMQGWRKNME DSHICYNNLK LNEIEEDISI
YGVFDGHGGP NVSKWISYNF RRIFLRCIKE ASEELTKKNI DKSKNYKLKL IKLTLEKTFL
KLDEEMLLTE NQEKLKKFSV PTQENEEESD TRENYLYSIL NDIISKNISI KAIERDGKRC
LQVVYNKDGN PVEEGSGDSV TSLTEDGRNN KSASMFDGTD GLTKGEEDDD EDDAEDAEDV
GDAEEDDFET VAVGTKEKNK GIEHMHESNN NALKKDDASS DCLNGSSNID VKAVKVEERE
EKNEGNVEKK YSSLVEKTDV AGKNSDVKGL QYKGKGEKNK GMDSGLLNLS KDNKNKIKEE
DNKEHSDYLD TDESTETNAK RLKKDMNNEY SNSEKEVNER EGKFTNSNEF NKTEKVKSEL
TYDNLKTLEK ETAMEKNNFG EDYDTNNSTN GNLSAYDENS LRLYEKVNSS SEEGFAYDET
VTNVIDNNIS SSNSENNNNN EGEDCNGVYS SDELRLFENY YSNDYEDNIA YSCGSTALVA
VILKGYLIVA NAGDSRAIVC FNGNSLGMST DHKPHLQAEE ARIKKAGGYI SNGRVDGNLN
LTRAIGDLHY KRDPFLPQKD QKISAFPEVT CVTLTPDDEF LFLACDGIWD CKDGQDVVGF
VKTRLDKFEE LNEDDKFLYN KESNADNITA TSATNDNIIF NGNNEDEESS KDTENNLSSH
ENANTGGNGS VNESTDVKNA NEGIKETADA HSDENKTNDI RNGLQENSDE ELEIERDGED
ETKYHSAPVI ERKKLDKFSK LSQICEELCD ECLSNNYKEN DGIGCDNMTC LIVQYNPFYK
IHTEKKFLNI DEIE
//
