KAPR_CANGA
ID KAPR_CANGA Reviewed; 404 AA.
AC Q6FQL6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR; OrderedLocusNames=CAGL0I05236g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380955; CAG60415.1; -; Genomic_DNA.
DR RefSeq; XP_447478.1; XM_447478.1.
DR AlphaFoldDB; Q6FQL6; -.
DR SMR; Q6FQL6; -.
DR STRING; 5478.XP_447478.1; -.
DR EnsemblFungi; CAG60415; CAG60415; CAGL0I05236g.
DR GeneID; 2889197; -.
DR KEGG; cgr:CAGL0I05236g; -.
DR CGD; CAL0132356; BCY1.
DR VEuPathDB; FungiDB:CAGL0I05236g; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; Q6FQL6; -.
DR OMA; YDNWSPP; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:EnsemblFungi.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IEA:EnsemblFungi.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
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; Reference proteome;
KW Repeat.
FT CHAIN 1..404
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205405"
FT REGION 27..169
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 43..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170..285
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
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 244
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 288..404
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 354
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 44964 MW; 83A09309536B9D14 CRC64;
MVSEECRSGL AAFQTAVNEN SPDDFFQYGA NYFNKKLEEQ RKLSRRSAVS GFKSPFASSD
PHAKESDNGL FKNSFGSGPF GGNDDPKSNS NSNDSGNGMR SQGQGPTDRN SPEALGNAPI
PNNFNALRRT SVSGETLQPD HFDDWQPEHY KEKSEEQLKR LEKSIGKNFL FNKLDSDSKK
LVINCLEEKR VSKGTEIIKQ GDEGDYFYVV ETGTVEFFVN NEKVNTSGAG SSFGELALMY
NSPRAATVVA QTDCTLWALD RLTFRKILLG SSFKKRLMYD DLLKNMEVLK SLSTYDRAKL
ADALDTKIYN AGDVIIREGD RGENFYLIEY GACDVTKEKE GLVTQLKDHD YFGEVALLND
LPRQATVTAT KRTKVATLGK SGFQRLLGPA VEVLKLNDPT RKHD
