ID   PTPA1_CRYNJ             Reviewed;         362 AA.
AC   P0CQ00; Q55JQ8; Q5K9U4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=CNK00750;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
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DR   EMBL; AE017351; AAW46120.1; -; Genomic_DNA.
DR   RefSeq; XP_567637.1; XM_567637.1.
DR   AlphaFoldDB; P0CQ00; -.
DR   SMR; P0CQ00; -.
DR   STRING; 5207.AAW46120; -.
DR   PaxDb; P0CQ00; -.
DR   EnsemblFungi; AAW46120; AAW46120; CNK00750.
DR   GeneID; 3254580; -.
DR   KEGG; cne:CNK00750; -.
DR   VEuPathDB; FungiDB:CNK00750; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_1_0_1; -.
DR   InParanoid; P0CQ00; -.
DR   OMA; LACRDWH; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000002149; Chromosome 11.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
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..362
FT                   /note="Serine/threonine-protein phosphatase 2A activator 1"
FT                   /id="PRO_0000226097"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  40468 MW;  B97735F85A57967C CRC64;
     MQPHTQPPQP EASSSRAVHI PSDPAPPRPC LTNDAIVSRW QSSPGFQYFW AWIKRRCDRL
     KGKEIIRGPF DHSAHGIRSL MNMLDQMTSW VEDATPQPQS NQRFGNLAFR TYNKLLQERL
     PPLIDSWDIP SNLRSQLLPL FINSHAFGHP TRLDYGTGHE LAFVLGLWCC VVPGWVGGDN
     GTEEEEDELI LRVFTRYLEL TTFLQKTYNL EPAGSHGVWG LDDYCFLPYL FGSAQLLGSN
     LTPSASLSLA LSHHPSATSP PSAPITDLYT LSLHHLTLFK FGASFSEHSP LLYSLSQMPN
     WVKPHGGLKK MFLGEVVGKR VVVQGIWVGG WCWGEDVPNV EERGDKNEGK GTDAGTKAPW
     AR