ID   PTPA1_ASPOR             Reviewed;         478 AA.
AC   Q2UN27;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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; ORFNames=AO090001000529;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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}.
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; AP007154; BAE57038.1; -; Genomic_DNA.
DR   RefSeq; XP_001819040.1; XM_001818988.1.
DR   AlphaFoldDB; Q2UN27; -.
DR   SMR; Q2UN27; -.
DR   STRING; 510516.Q2UN27; -.
DR   EnsemblFungi; BAE57038; BAE57038; AO090001000529.
DR   GeneID; 5991011; -.
DR   KEGG; aor:AO090001000529; -.
DR   VEuPathDB; FungiDB:AO090001000529; -.
DR   HOGENOM; CLU_030733_2_0_1; -.
DR   OMA; SWDRDPN; -.
DR   Proteomes; UP000006564; Chromosome 2.
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   SUPFAM; SSF140984; SSF140984; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..478
FT                   /note="Serine/threonine-protein phosphatase 2A activator 1"
FT                   /id="PRO_0000226094"
FT   REGION          359..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  52116 MW;  86FC23D8B26204F4 CRC64;
     MAADGLPVRV LPTLDPSEGH TFLEPSKRIN EGDDVSEFLC SKAYVDIMTF LLQLNRSMFP
     AKLPDGRVQT WPLNTEAVGF SAPVRQLQQL LSKIEDLLDA TPLMPGEWRY ANGAFQVWHD
     KVKKATPSLL AECLPAEILH APSSDPNGPT AEVELTEYFL GSWGSRERMD YGTGHELSFL
     TFLGAIWKLN GFPKNEPGVE ERTIVLGVIE PYLELIRAVI KKYKLEPAGS HGVWGLDDHS
     FIPYIFGSAQ LGPAISNSDL VPETGSLPDA VDPDGVTKAN VVEKERKVNM YFSAIGFIND
     VKKGPFWEHS QMLYNISGVQ AGWAKINKGM IKMYNAEVLS KFPVVQHFRF GSLFSWNRDP
     SAIPPPSRIH TSSGPETRPR QVPPSARQDP GPGTKAPWAT ASQSTPPPST GTAAPWATSR
     AGREPPTTSR IPSALPDTSR LPPGPMAPTR APWASSQPAG PAPTGDPNDI TTKAPWAK