ID   PTPA1_EMENI             Reviewed;         432 AA.
AC   Q5B6C5; C8V6A0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
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; ORFNames=AN3905;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000063; EAA58836.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF75125.1; -; Genomic_DNA.
DR   RefSeq; XP_661509.1; XM_656417.1.
DR   AlphaFoldDB; Q5B6C5; -.
DR   SMR; Q5B6C5; -.
DR   STRING; 162425.CADANIAP00004793; -.
DR   EnsemblFungi; CBF75125; CBF75125; ANIA_03905.
DR   EnsemblFungi; EAA58836; EAA58836; AN3905.2.
DR   GeneID; 2873327; -.
DR   KEGG; ani:AN3905.2; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_2_0_1; -.
DR   InParanoid; Q5B6C5; -.
DR   OMA; SWDRDPN; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
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:0006914; P:autophagy; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
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..432
FT                   /note="Serine/threonine-protein phosphatase 2A activator 1"
FT                   /id="PRO_0000226099"
SQ   SEQUENCE   432 AA;  48232 MW;  BB912EB474B90D12 CRC64;
     MDTSQVRILP KLDISAGHNF TKPSKRINES QDVAEFLSSK AYVDLMTFLL QLNRSLFPTK
     LPDGRVLTWE LNSEAVEYSA PVRQLQQLLS KLEAILDEAP PDTGPRRFGN ISFRRWYEMV
     ESRAASLLEE CLSKEILQMP SSDPGAPTAE VELLAYFLGS WGSPQRLDYG TGHELSFLAF
     LAGIWKLHGF PENSPGVEER AIVLGVIQPY LELVRTIIKR YTLEPAGSHG VWGLDDHSFI
     PYIFGSAQLA PAISESDRIP EEGSLSDAPA PGGVTKANVV ERERKHNLYF SAIGFIYDVK
     RGPFWEHSPM LYDISGIQAG WAKINKGMIK MYNAEVLSKF PVVQHFPFGS LFSWERDPNA
     PSPAADAHIA ATTRRTDEAS TSSYLYSPKY IKATSWSYGS YKGALGNIST RWTGSPWRFY
     VCRPYANESS VG