ID   KAPR_BLUGR              Reviewed;         389 AA.
AC   Q9HEP7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
GN   Name=pkar; Synonyms=bkr1;
OS   Blumeria graminis (Powdery mildew) (Oidium monilioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=34373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bindslev L.;
RL   Thesis (2001), University of Copenhagen, Denmark.
CC   -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC       subunits. In the presence of cAMP it dissociates into 2 active
CC       monomeric C subunits and an R dimer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; AJ304829; CAC19660.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HEP7; -.
DR   SMR; Q9HEP7; -.
DR   PRIDE; Q9HEP7; -.
DR   VEuPathDB; FungiDB:BGT96224V316_LOCUS2241; -.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Repeat.
FT   CHAIN           1..389
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205403"
FT   REGION          1..128
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..258
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         207
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         261..377
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         327
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  42559 MW;  C8E6F38E21CE7B5F CRC64;
     MSENTFPGRL GINPFGPESR AANTEKPSTS HIVRVTERDE DKVNPTFNNK PLKKFAGDRA
     TNTPLQAFKL GASDGFPEHY GMGRRTSVSA ESLNPNPTAS SNESWTPPYH RKTPEQLERL
     KKSISGNFLF NHLDDEQSAQ VLGALVEKPI PVKDIKVISQ GDQGDFFYVV EKGSFDVYVN
     PAGSVQPGLG GLGNKVATIE PGGSFGELAL MYNAPRAATV ISAEGSCTLW SLDRITFRRI
     LMDSTFKCRR LYESFLEEVT LLSTLTKYER SKIADALVTL KYPAGTTIKE GDVGEEFYLL
     ESGEAEAFKA GCQNAVKCYS KGDYFGELAL LNDAPRAASV VSKTEVKVAK LGKDGFQRLL
     GPVESIMRRT KYEGVEEIDR EFPGSAAAL