ID A0A0V0R3A6_PSEPJ Unreviewed; 479 AA.
AC A0A0V0R3A6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-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_08191 {ECO:0000313|EMBL:KRX08988.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX08988.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX08988.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX08988.1};
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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:KRX08988.1}.
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DR EMBL; LDAU01000056; KRX08988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R3A6; -.
DR EnsemblProtists; KRX08988; KRX08988; PPERSA_08191.
DR InParanoid; A0A0V0R3A6; -.
DR OMA; NHFFMSR; -.
DR OrthoDB; 1107740at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07417; MPP_PP5_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041753; PP5_C.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PIRSF; PIRSF033096; PPPtase_5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 7..40
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 78..111
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 186..462
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|SMART:SM00156"
SQ SEQUENCE 479 AA; 55011 MW; FFCF421F21FEB4AA CRC64;
MEENKTAEEC KNEGNNYFKK SEYPQALEWY NKAYELDSDS TKAAVYLSNR SFCHLKMENF
GLAIADANLA EEKDPKYVKA FYRQGQALFL LGKLEEARNS FLKAKKLLPS DADIIKKLKI
LKELITKKKF EEAISVPDAP KDLDLNWEEM TVPSSYDGPR METLDEPITS EWCVKLMDHM
KDQKKLHKKY VTMLLIRAKE ILKAQETLVD FEVPEGQEIT VCGDTHGQYY DLLNIFSING
NPSDTNPYLF NGDFVDRGSF SVEVMLCLLA WKVSNPNAMH LTRGNHETRN MNKLYGFEGE
VIAKYDQKTF EFFSDIFWYL PLAYVLNKTV QVNHGGLFQQ DGVKLDQIRK INRFGEPPES
GLFSDIIWSD PSESPGRTMS KRGVSCQFGP DITKKYLEDN GLSLLVRSHE MKQEGYEEQH
NGKCITIFSA PNYCDQMGNK GAFIRFKGGE MKPKFTQFTA VEHPKVPPMA YAKSFYNMF
//
