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Database: UniProt
Entry: A0A0V0QM10_PSEPJ
LinkDB: A0A0V0QM10_PSEPJ
Original site: A0A0V0QM10_PSEPJ 
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
//
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