ID   B8MAS1_TALSN            Unreviewed;       665 AA.
AC   B8MAS1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   03-MAY-2023, entry version 54.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN   ORFNames=TSTA_115570 {ECO:0000313|EMBL:EED17760.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17760.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC       and catalytic activity, and also might direct the localization of the
CC       catalytic enzyme to a particular subcellular compartment.
CC       {ECO:0000256|PIRNR:PIRNR028043}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit.
CC       {ECO:0000256|PIRNR:PIRNR028043}.
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DR   EMBL; EQ962655; EED17760.1; -; Genomic_DNA.
DR   RefSeq; XP_002481752.1; XM_002481707.1.
DR   AlphaFoldDB; B8MAS1; -.
DR   GeneID; 8099584; -.
DR   VEuPathDB; FungiDB:TSTA_115570; -.
DR   OMA; DGTEDNQ; -.
DR   OrthoDB; 5473951at2759; -.
DR   PhylomeDB; B8MAS1; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; SERINE/THREONINE PROTEIN PHOSPHATASE 2A PP2A REGULATORY SUBUNIT B; 1.
DR   PANTHER; PTHR10257:SF3; WELL-ROUNDED, ISOFORM B; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   REGION          1..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  75626 MW;  7ECF879512A90F4D CRC64;
     MKGFRQRVHE QLSRAKDSNK SSKKRDSNNN TSNTGLSPAH HAQSTSPNHV TPTSSTTSLN
     ETRNAKVDNA SPAAINSPAG HQNNQGAAAP AGAGQHFVPS AQSMGGNLGG QPANLPGTPT
     RQGQQPITPS VVISPSSHVP LPGAAETMPG DLAPPKKSHV FDRLHSTPKD MSEGIRTPKR
     QHSSRFDISD QRQRELEKLP GFHEVPPNRR QDLFMQKIDQ CNIIFDFNDP TADMKSKEIK
     RLALHELLDY VANNRSVITE PMYPRVVDMF AKNLFRPIPP PVTPQGEAYD PEEDEPVLEV
     AWPHIQVVYE FFLRFIESQD FNTNIAKQYI DHQFVLQLLE LFDSEDPRER DFLKTTLHRI
     YGKFLNLRSY IRRSINNVFF QFTYETERFN GIAELLEILG SIINGFALPL KEEHKLFLTR
     VLIPMHKPKG LSMYHPQLAY CIVQFLEKDS VLTEDVVMGL LRYWPKVNST KEVMFLNEVE
     DIFEVMDPTE FAKVQGPLFT QLAKSVASPH FQVAERALYF WNNEYFCNLV SDNVETILPI
     MFAPLYENSK GHWNRTIHSM VYNAMKLFME INPQLFDECS QEYNEHQSGA EEREQARRRR
     WEVLAEQAEK RKKGLLKEPT TSTTSVPASK ADDIDPVTQD SQKRLNALKL DETTTVKDRA
     TTSPS
//