ID   PTPA1_DEBHA             Reviewed;         441 AA.
AC   Q6BNW4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A activator 1;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-1;
DE            Short=PPIase PTPA-1;
DE            Short=Rotamase PTPA-1;
DE   AltName: Full=Phosphotyrosyl phosphatase activator 1;
GN   Name=RRD1; OrderedLocusNames=DEHA2E18502g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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; CR382137; CAG88373.2; -; Genomic_DNA.
DR   RefSeq; XP_460106.2; XM_460106.1.
DR   AlphaFoldDB; Q6BNW4; -.
DR   SMR; Q6BNW4; -.
DR   STRING; 4959.XP_460106.2; -.
DR   EnsemblFungi; CAG88373; CAG88373; DEHA2E18502g.
DR   GeneID; 2902052; -.
DR   KEGG; dha:DEHA2E18502g; -.
DR   VEuPathDB; FungiDB:DEHA2E18502g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_2_1_1; -.
DR   InParanoid; Q6BNW4; -.
DR   OMA; LACRDWH; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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   CDD; cd04087; PTPA; 1.
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; 1.
DR   Pfam; PF03095; PTPA; 1.
DR   PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR   SUPFAM; SSF140984; SSF140984; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..441
FT                   /note="Serine/threonine-protein phosphatase 2A activator 1"
FT                   /id="PRO_0000226098"
FT   REGION          66..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  50486 MW;  2B6C14F13B87FB2E CRC64;
     MSNTHNIHWS TPSKRIYDAS DIPNFKRSIA YYKIRHTLSV VIEKVKGCDL PPGILDKSIV
     TRKINNIPPS NTTHSRPLDL PPPQGEEEGD KCNISHSSNQ TIRGEANESN YEGLLRILEV
     LNRYIDETPP LKGPRRFGNL ACRDWHEKMN TKMNDLLKDN IKIHNSSFNS EFDGFIKELK
     YYIENSFGSA IRLDYGTGHE LSFLAFIGGL IDFKLLSLEE LTGSDILTIF AKYYDLTRRL
     ILVYSLEPAG SHGVWGLDDH YHLIYIFGAA QFNGDQDKII PPVQQILTRP VLDRYKETNL
     YVNAISFIHK IKSGPFNEHS PIIFDIHSSV SLWSKVLSGL LKMFEVEVLG KFPVVQHFWF
     GSSLYPWRDF ETNKELPIYK RDEDEMDEDS SGDFLNGNTG IKTTKHNISM TGAPWNLNAT
     QRQDDLNSTT YRGRQPRLGR N