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Database: UniProt
Entry: G8BB98_CANPC
LinkDB: G8BB98_CANPC
Original site: G8BB98_CANPC 
ID   G8BB98_CANPC            Unreviewed;       648 AA.
AC   G8BB98;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Protein phosphatase PP2A regulatory subunit A {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CPAR2_808710 {ECO:0000313|CGD:CAL0000148323,
GN   ECO:0000313|EMBL:CCE42322.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE42322.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC       {ECO:0000256|ARBA:ARBA00038332}.
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DR   EMBL; HE605205; CCE42322.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8BB98; -.
DR   STRING; 578454.G8BB98; -.
DR   EnsemblFungi; CPAR2_808710-T; CPAR2_808710-T-p1; CPAR2_808710.
DR   CGD; CAL0000148323; CPAR2_808710.
DR   VEuPathDB; FungiDB:CPAR2_808710; -.
DR   eggNOG; KOG0211; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 8.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR   GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0030952; P:establishment or maintenance of cytoskeleton polarity; IEA:EnsemblFungi.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection in anaphase I; IEA:EnsemblFungi.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IEA:EnsemblFungi.
DR   GO; GO:0006417; P:regulation of translation; IEA:EnsemblFungi.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   PANTHER; PTHR10648:SF4; PROTEIN PHOSPHATASE 2 (FORMERLY 2A), REGULATORY SUBUNIT A, BETA ISOFORM-RELATED; 1.
DR   PANTHER; PTHR10648; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A 65 KDA REGULATORY SUBUNIT; 1.
DR   Pfam; PF02985; HEAT; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 9.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          45..82
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          84..121
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          161..198
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          295..327
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          339..377
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          378..416
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          417..455
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          565..602
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          616..648
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REGION          507..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   648 AA;  73540 MW;  507C4AF6B30B5CE7 CRC64;
     MDDLYPLALL MDELKHDDVS NRVEAMQKLD TIAIALGPER TRKELLPFLH DVAQDDEEEV
     FTVLGAKLGE FIPLIGGHEY CEPLIEILTI LASMEEPLVR DKAIESLNQI SQELNQDEIN
     NVFLGLITGL SQGNWFSKKI ASCGLYKAVI IRVDANTRKE LLRTYLKLVT DDYPMVRRAA
     ATNLPHLIDL LTKFTEESPN DVNKVNNEDW EIISKMFQHL INDDQDSVKF LSVDVLIAIL
     EFFQKIHEYS FNSDFLSSAL KLIKDDSWRV RYTAADRFSK IAINFTHNES DLFQLIDPFI
     SLMKDHEGEV RKAIAKQLPG FCKLLTEYPP TKATILNKIV PVVNELSQDP QENVRASLAS
     TITELSPILT RQPTIDKLLP IFLTMLKDEF PDVRLNIISN LSVVNETIGI NLLSTNLLPA
     ITELAQDHKW RVRLAIIEYI PKLADQLGQS FFNNELLSLC MSWLWDPVFA IREAAVENLK
     NLTVIFGSQW ATEEILSRLL NKRNSKMDED GSGVGNGNNT GDENDDDDDD DNKIDYSNFI
     IRITCLFAIT SLIPVINYSV LVDKVLPFIN GLITDSVPNI RFNVAKSYLT LVQSLIQQRN
     QAPNEDELKK LINLQVLSNL EKLESDEDVD VRFYSTQSIK GINEILAQ
//
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