ID   KAPR_HYPAT              Reviewed;         462 AA.
AC   Q86ZN7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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=pkar1;
OS   Hypocrea atroviridis (Trichoderma atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=63577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zeilinger S., Kubicek C.;
RT   "Trichoderma atroviride cAMP-dependent protein kinase regulatory subunit.";
RL   Submitted (JAN-2002) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF473578; AAO33461.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86ZN7; -.
DR   SMR; Q86ZN7; -.
DR   OMA; REAVSHN; -.
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; 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..462
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205415"
FT   REGION          54..203
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          79..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         204..333
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         282
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..453
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         401
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         410
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  50151 MW;  8281DDE474ABA145 CRC64;
     MSLPEAYQLE IQALNKQVLQ TCPSDILQFC ADFFNSRLAT ERAASISLFR DRGTPSPRFP
     PSPTNPHFGM MSSQFSSPFG ANANPFGGSS SNPNPFGGSA SPMSSSVMHR VVEEDESDNH
     LAPGGSLFSG AFGGDASTEA PPTLRAPPTT DSYPAQYNFS RRTSVSAESL KPSADGFDNW
     TPPYTDKTPE QVERLKYAIE GNFLFSHLDD EQSAQILGAL VEKPIPARGI KVISQGDAGD
     YFYVVERGSF DVYVNDCGFI EPGPDGLGNK VGTIQAGGSF GELALMYNAP RAATIISAEG
     SCTLWALDRV TFRRILMEST FARRRMYENF LEEVPILSSL TPYERSKISD ALETQKFAPG
     DVIIHEGDPG HSFYLLESGE AAAFKGEEQV LSYKKGDFFG ELALLNDAPR AASVIATSDV
     KVATLGKNAF QRLLGPVEGL LRRTRYLGVK TGVEEMDPLH TQ