ID S3DE05_GLAL2 Unreviewed; 679 AA.
AC S3DE05;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN ORFNames=GLAREA_11454 {ECO:0000313|EMBL:EPE24873.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE24873.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE24873.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145372; EPE24873.1; -; Genomic_DNA.
DR RefSeq; XP_008087788.1; XM_008089597.1.
DR AlphaFoldDB; S3DE05; -.
DR STRING; 1116229.S3DE05; -.
DR GeneID; 19470495; -.
DR KEGG; glz:GLAREA_11454; -.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_1_2_1; -.
DR OMA; DGTEDNQ; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000016922; 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:UP000016922}.
FT REGION 1..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 77081 MW; B8CC2BD4F194A929 CRC64;
MNRFRQKVHE QLSRAKDPSK SSKSKNKDSK DGTSSPSQSS SSRDAGQSPV ATPSSSTTTL
SDPRNKPLPP NDGGASSPAP QPQSGSIGSL NPSHSTLSAP DRFNSTMNVS PANSSGPGTP
NRHGPPSVVI SPSTPHIPPP GAAETMPQDL APPKAGQKSL MFHGLSTTPK DVPEGLRTPK
RQHSSRFDIS PQRELEKLPG FHEVPPNRRQ ELFMQKIDQC NVIFDFNDAS GDMKSKEIKR
LALHELLDYV ANNRQVITES MYPRVVEMFS KNLFRPIPPP MNPQGEAFDP EEDEPVLEVA
WPHIQVVYEF FLRFIESQDF NTNIAKAYID HSFVLQLLEL FDSEDPRERD FLKTTLHRIY
GKFLNLRSYI RRSINNVFFQ FIYETERFNG IAELLEILGS IINGFALPLK EEHKLFLTRV
LIPLHKVKSL SMYHPQLAYC IVQFLEKDAA LTEEVVLGLL RYWPKVNSTK EVMFLNEVED
IFEVMDPAEF AKVQEPLFHQ LAKSVASPHF QVAERALYFW NNEYFCNLVS DNVEIILPIM
FAPLYENSKG HWNRTIHGMV YNAMKLFMEI NPQLFDDCSH DYTEHQNNAE AREQARENKW
KALVDQANRS NTNGVVRPGA ISSPSRNKVS APLRIDEVDP ITEDNQKRLD SLKLQDADRR
DRRPTHDRQN SVGSSRSQR
//
