ID J9W494_CRYNH Unreviewed; 708 AA.
AC J9W494;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN ORFNames=CNAG_05634 {ECO:0000313|EMBL:AFR99065.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR99065.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR99065.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003833; AFR99065.1; -; Genomic_DNA.
DR RefSeq; XP_012053893.1; XM_012198503.1.
DR AlphaFoldDB; J9W494; -.
DR GeneID; 23888932; -.
DR KEGG; cng:CNAG_05634; -.
DR VEuPathDB; FungiDB:CNAG_05634; -.
DR HOGENOM; CLU_012437_1_1_1; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000010091; Chromosome 14.
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;
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 80059 MW; FF420C38CD3005FC CRC64;
MKGLKKAMNL SRTKSSEKSK SPNPPAHKQS AVSSGPSSPS VNSPNRQAPD APALQGGAPI
TPRRSPINDK TSPAPPLVVI SGAPQAPPIN TEMPSDPIPH SPHGRYGSPE RSLGADGQPT
PPKVGPMNRL RGPKDTIPAV GKTPRKQRSS RFYVTEKVEI EKLPNFADVR PEQRNELFVQ
KLQQCRVLFD FNDASSDLEG KQIKSQTLHE MLEYITSQRG VITESIYPEV VSMFATNLFR
SIPPQVNPTG DAFDPEEDEP VLELAWPHLQ IVYEFFLRFV ESPDFNTNIG KRYIDQSFVL
QLLELFDSED PRERDFLKTT LHRIYGKFLN LRAFIRRSIS HVFFQFVYET ERHNGIAELL
EILGSIINGF ALPLKEEHKT FLTRALIPLH KAKSLALYHP QLAYCVVQFL EKDPALTEEV
VLGLLRYWPK VNSPKEVMFL NEVEEILDVI EHNEFIKIMQ PLFVQLARCI NSAHFQVAER
ALYYWNNEYI VNLMGEHISI ILPIVFPALY QNSKTHWNRT IHGMVYNALK LFMEINQEVF
EECQNNYRAQ RKAESDRAIE RYDEWLQLRE QAIQNWETSH PSSPLPERLQ EPPPPRPEPY
EDEPMMDVSV DMTANGFDPS ESFTLDRSIG EEMVPVADPG VDKAPSLSPT SPTQLLGQQG
QAPSSPTPSG GGGTAPHLRR KSVLPIDAGV MRDLQNHRSL ENEANPEP
//