ID   G3JP31_CORMM            Unreviewed;       762 AA.
AC   G3JP31;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN   ORFNames=CCM_07893 {ECO:0000313|EMBL:EGX89641.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX89641.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX89641.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX89641.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126404; EGX89641.1; -; Genomic_DNA.
DR   RefSeq; XP_006673096.1; XM_006673033.1.
DR   AlphaFoldDB; G3JP31; -.
DR   STRING; 983644.G3JP31; -.
DR   GeneID; 18169903; -.
DR   KEGG; cmt:CCM_07893; -.
DR   VEuPathDB; FungiDB:CCM_07893; -.
DR   eggNOG; KOG2085; Eukaryota.
DR   HOGENOM; CLU_012437_1_2_1; -.
DR   InParanoid; G3JP31; -.
DR   OMA; IVSGHEQ; -.
DR   OrthoDB; 5473951at2759; -.
DR   Proteomes; UP000001610; 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:UP000001610}.
FT   REGION          123..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  86516 MW;  668DA6DF97D87E63 CRC64;
     MVISSAVPRL QRLHQYIPSS SYKYSSCNSS SHMRLQSGPI ATRLLAKHTL ILADILSPYC
     RQQAKVFIFA CALVPSARDA LTSGWHRCPR STAALSPYPA RATTVPPEQY MGEQLQDKMK
     RFSQKVLSRG KDSTKSSKKN KDTKDGTASP SSRDPSTQSP TLTPTSSTTA VNDIRNKPLP
     PNSTDGLGQS AGVDRFGAMG ANSSPNGNSR MPPTVVISPT PGHVPPPGAA ETMPHDLAPP
     KSGQKSLMIH RGIDNRDAIP EGLRTPKRQH SSRFDISTNR DLEKLPGFHE VPPNRRQELF
     MQKIEQCNVI FDFNDASGDM KAKEIKRLAL HELLDYVANN RQVITEPMYP KVVDMFSKNL
     FRPIPPPMNP QGEPFDPEED EPVLEVAWPH IQVVYEFFLR FIESQDFNTN IAKAYIDHSF
     VLQLLDLFDS EDPRERDFLK TTLHRIYGKF LNLRSFIRRS INNVFFQFTY ETERFNGIAE
     LLEILGSIIN GFALPLKEEH KIFLTRVLLP LHKPRSLSMY HPQLAYCIVQ FLEKDASLTE
     DVVLGLLRYW PKVNSTKEVM FLNEVEDIFE VMDPAEFAKV QEPLFHQLAK SVASPHFQVA
     ERALYFWNNE YFCNLVSDNV EIILPIMFAP LYENSKGHWN RTIHGMVYNA MKLFMEINPQ
     LFDDCSHEYT EHQNSAAERE ALRERKWAAL GEQAESRRNS MASDVGEPPQ RTQVTAMPRV
     DEADQGADDS QKRLDSLRLQ DQSGRRPSVH ERQGSTSSTR SR
//