ID   PTPA_ENCCU              Reviewed;         247 AA.
AC   Q8SVB5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A activator;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA;
DE            Short=PPIase PTPA;
DE            Short=Rotamase PTPA;
DE   AltName: Full=Phosphotyrosyl phosphatase activator;
GN   OrderedLocusNames=ECU06_0720;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases
CC       modulating their activity or substrate specificity, probably by
CC       inducing a conformational change in the catalytic subunit, a direct
CC       target of the PPIase. Can reactivate inactive phosphatase PP2A-
CC       phosphatase methylesterase complexes (PP2Ai) in presence of ATP and
CC       Mg(2+) by dissociating the inactive form from the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR   EMBL; AL590446; CAD25432.1; -; Genomic_DNA.
DR   RefSeq; NP_585828.1; NM_001041450.1.
DR   AlphaFoldDB; Q8SVB5; -.
DR   SMR; Q8SVB5; -.
DR   STRING; 284813.Q8SVB5; -.
DR   GeneID; 859252; -.
DR   KEGG; ecu:ECU06_0720; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0720; -.
DR   HOGENOM; CLU_030733_4_0_1; -.
DR   InParanoid; Q8SVB5; -.
DR   OMA; WRISKYF; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000000819; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019211; F:phosphatase activator activity; IEA:InterPro.
DR   Gene3D; 1.20.120.1150; -; 1.
DR   InterPro; IPR004327; Phstyr_phstse_ac.
DR   InterPro; IPR043170; PTPA_C_lid.
DR   InterPro; IPR037218; PTPA_sf.
DR   PANTHER; PTHR10012; PTHR10012; 2.
DR   Pfam; PF03095; PTPA; 2.
DR   PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR   SUPFAM; SSF140984; SSF140984; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..247
FT                   /note="Serine/threonine-protein phosphatase 2A activator"
FT                   /id="PRO_0000226121"
SQ   SEQUENCE   247 AA;  28843 MW;  DC51586F7CFF9DA8 CRC64;
     MKNGIDFVET EAYARIYNFI LMVDDSIKNS EQRQSKHHMD VLADITRIVS ETEKDPSPQR
     YANMAAKTVF KKIYDTYDDE YLRNSFGNQI RLDYGTGHEL NFLCYLYAQY CRGSIGIDCV
     FTILVKYFEI VRLFITKFNL EPAGSHGMWG LDDYQFLPFL FGSSELCNTT LRFDELDGSK
     CYFVAVEKKL GGSSRILKSI MDKDWASINR GMIRMYDDHV LRRSVVTQHF IYGEYLRKDR
     SQANKDL