ID   KAPR_ASPNG              Reviewed;         411 AA.
AC   Q9C196;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
GN   Name=pkaR;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RA   Staudohar M., Bencina M., Van de Vondervoort P., Legisa M., Panneman H.,
RA   Ruijter G., Visser J.;
RT   "Cyclic AMP-dependent protein kinase is involved in morphogenesis of
RT   Aspergillus niger.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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; AJ296317; CAC36308.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9C196; -.
DR   SMR; Q9C196; -.
DR   STRING; 5061.CADANGAP00012604; -.
DR   VEuPathDB; FungiDB:An16g03740; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1091608; -.
DR   VEuPathDB; FungiDB:ATCC64974_70150; -.
DR   VEuPathDB; FungiDB:M747DRAFT_23407; -.
DR   eggNOG; KOG1113; Eukaryota.
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; 2.
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..411
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205401"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          23..159
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..289
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         238
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         292..411
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         359
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  44522 MW;  BA43E6C393F09706 CRC64;
     MAESAFPSAQ QPLRVGTKDD KAAAFQKISE EDEYEVTSPT DPTFRSANAA AASSSTGSPF
     FGGSYGENSG PIRFNRSPFD NGPREEDEEG ADEFPPEDIR PTGAANQGFP NNYALGRRTS
     VSAESLNPTS AGSDSWTPPY HEKTEEQLSR LKTAVSSNFL FSHLDDDQFK SVLDALVEKP
     IPAKGIKVIS QGDAGDYFYI VENGHFDFMI HPSGSVQPGP DGMGNKVGSV GPGGSFGELA
     LMYNAPRAAT VVSVDPKSTL WALDRITFRR ILMDSAFQRR RMYEAFLEEV PLLSSLKPYE
     RAKIADALDA IKYPAGSTII AEGDPGDAFY LLESGEADAF KNGVEGPVKS YKRGDYFGEL
     ALLDDKPRAA SIVAKTDVKV AKLGRDGFKR LLGPVEDIMR RAEYESNPVP A