ID A0A0V0QM10_PSEPJ Unreviewed; 959 AA.
AC A0A0V0QM10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PPERSA_08656 {ECO:0000313|EMBL:KRX03359.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03359.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03359.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03359.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- FUNCTION: Enzyme with a broad specificity.
CC {ECO:0000256|ARBA:ARBA00003302}.
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 Evidence={ECO:0000256|ARBA:ARBA00001512};
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- 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:KRX03359.1}.
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DR EMBL; LDAU01000134; KRX03359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QM10; -.
DR EnsemblProtists; KRX03359; KRX03359; PPERSA_08656.
DR InParanoid; A0A0V0QM10; -.
DR OMA; IFREQMA; -.
DR OrthoDB; 276784at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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; PTHR47992:SF233; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00481; PP2C; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000054937}.
FT DOMAIN 404..672
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..884
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 112061 MW; 8EFCF9E12EC48398 CRC64;
MYSRKENQGK YNQINNSYNP KLKLESESVK GSYNPLKNQL QNLYPESSTS ASYASKYNYQ
YQPQTSQSQQ FQLGYFAQKQ QAQNPQKSYD VRPYSASMNM PYSATNQQYM HSNISKQFWA
GNATTKNDNL KNVNKFSDFY NFQNQNLNQN LHQQNSQQQQ KQQSLLQSQK YQENLRKQSR
DLSSLMEREE SPTLKKKQFS EQHSQFYSQN PSNNLNSNLS NNLNNNQNNN NNKQVAQSIQ
FNTNNEVHKA DKNSYSLGSS LYQSANTEQF SKLQAKKQQQ QQQQQQNNFQ QQQQQQQQQN
NLQQQQQQQQ MEIEQEEQQE PSHSLSKNQQ PNYYELKRKH QSMQYKKNPS LSQQQENNNN
NNNNTNNNNN NSNNNNQKLF EAGEPLPNQE PTKCSFKRSG IVKAYAANTN QGLVRNYNED
RVSIILNIMK PQSRQQETWP KCSFFGVYDG HGGVMCADFL RDNLHQYVIK EPSFPWNPKE
ALKNGFKAAE SQFLEMAQNK EIFREQMAQK LILFLETISL AMNRNKLELP KEGGKFISKT
QAQTTKMGPN NKTYNQLLLG PLRVFPGRLS VSRTFGDIEA KLEKFGGNPN VVICDPEIKS
FKITDDQDFI ILASDGIFDK LSSREAIQQV WESTNEKQPN IHKQCGLGVE YILRESLNQK
SLDNVTVVMI AFQNFKTKLF GQSSQKTQKS IQQSQTVQPS KNQSNQNQKM PLEERSLNIQ
NQQPNQLQLQ QQQQQQMEKN LKQSQYQSKQ NENLPKQQIQ NQNQNQNYNQ NQNQNQNSAS
VQHLNLQQQS YRKNNNNNKQ VSSSYQNFSQ KLQQNQQFLE QQLNSRTKKK SIENTNLNRN
AVSISYRDQS SLQEKAKKQQ QQQLQQQQQQ LQQQQQQLQQ QQQNNFSSQN YASLHGRKNS
MKENINYDLN QNLNQNYNQN FQQNKMKLLD QKISEISSKV NQFSMLENYS KIRGSYMQK
//