ID   KAPR_MUCCL              Reviewed;         427 AA.
AC   Q8TF77;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
GN   Name=pkar;
OS   Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=29924;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX   PubMed=12702308; DOI=10.1111/j.1567-1364.2002.tb00085.x;
RA   Wolff A.M., Appel K.F., Breum J., Poulsen U., Arnau J.;
RT   "Identification and analysis of genes involved in the control of dimorphism
RT   in Mucor circinelloides (syn. racemosus).";
RL   FEMS Yeast Res. 2:203-213(2002).
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; AJ400723; CAC81804.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TF77; -.
DR   SMR; Q8TF77; -.
DR   PRIDE; Q8TF77; -.
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; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Repeat.
FT   CHAIN           1..427
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205413"
FT   REGION          38..184
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          96..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..126
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         185..300
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         250
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..422
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         372
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  48699 MW;  894BA6DF650523AE CRC64;
     MITDEHPFEF APQQDEYTQL LTELHNEYCA EQPLDVLQFC SNFFIRKLEE QRLEHRNNHH
     SRNNLFDTND TSNDLHPLCE QPQEDFSQQQ GIQWETTHMG HPNDHGALHD DDDDPLEDED
     DEEFDKFSTE PLPSLPPTNY NRGRRTSVKC REHGTQRQPR LCQGHHPQIS GTSERIKVSI
     SNNFLFRNLD EEQYLDVVNA MSEKRVVKGT TVIEQGSVGD FFYVVESGTL DCFIGQNKVT
     NYEAGGSFGE LALMYNAPRA ATIITTSDSV LWALDRNTSA PSLMENTSRK RRMYEYFLSE
     VVLLKSLESY EQHKIADALE SVYFEDGQEV VKQGDVGDQF YIIESGEAIV LKEENGVQQQ
     VNQLERGSYF GELALLNDAP RAATVVAHGR LKCATLGKKA FTRLLGPVLD ILKRNSENYH
     AVINQQS