ID   KAPR_BLAEM              Reviewed;         403 AA.
AC   P31320;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
GN   Name=PKAR;
OS   Blastocladiella emersonii (Aquatic fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Blastocladiella.
OX   NCBI_TaxID=4808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1512258; DOI=10.1016/s0021-9258(18)41913-8;
RA   Marques M.V., Gomes S.L.;
RT   "Cloning and structural analysis of the gene for the regulatory subunit of
RT   cAMP-dependent protein kinase in Blastocladiella emersonii.";
RL   J. Biol. Chem. 267:17201-17207(1992).
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 that binds four cAMP molecules.
CC   -!- DEVELOPMENTAL STAGE: Protein kinase activity is low in vegetative
CC       cells, rising sharply during sporulation; during germination its
CC       activity decreases to its original level.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; M81714; AAA33016.1; -; mRNA.
DR   EMBL; M81713; AAA33015.1; -; Genomic_DNA.
DR   PIR; A43435; A43435.
DR   AlphaFoldDB; P31320; -.
DR   SMR; P31320; -.
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; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
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   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   2: Evidence at transcript level;
KW   cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Repeat.
FT   CHAIN           1..403
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205402"
FT   REGION          1..155
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          79..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..104
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..278
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         226
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         279..403
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         349
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         372
FT                   /note="K -> T"
SQ   SEQUENCE   403 AA;  44468 MW;  4FFFEF48B27B2A40 CRC64;
     MADYTIPSEL PPILKDLSRE VLRHQPADLV QFCHDYFAKL LAQQRKVLMD SADPATKATI
     ASTAGPAVDA DEAARANSYA YSTDDGFGTE DDDDDDDDED DEAAIPPPVV NRGRRTSVSA
     ESMAPTAHDV DAVKTVIPKS DEQRARIQAS IGNNFLFRNL DEDQYTDVVN AMAEKKVAAG
     EVVIRQGGVG DYFYVVETGA LDVFVNRNGN GDVKVTDYSA GGSFGELALM YNAPRAATVV
     ATAESVLWAL DRVTFRRILM DHTSRKRRMY EAFLEEVPLL SSLEPYERHK IADALESVAY
     ADGDVVIRQG DVGENFYIIE AGDAEVIKID ENGEEHHFRP LHKGNYFGEL ALLSDKPRVA
     TIRAKGKLKC AKLGKKAFTR LLGPLADIMQ RNTQDYEKYP GEH