ID A0A1G4IP83_9SACH Unreviewed; 461 AA.
AC A0A1G4IP83;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit {ECO:0000256|ARBA:ARBA00020355, ECO:0000256|PIRNR:PIRNR000548};
GN ORFNames=LADA_0A05952G {ECO:0000313|EMBL:SCU78504.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU78504.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|EMBL:SCU78504.1, ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU78504.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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. {ECO:0000256|PIRNR:PIRNR000548}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753, ECO:0000256|PIRNR:PIRNR000548}.
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DR EMBL; LT598460; SCU78504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4IP83; -.
DR STRING; 1266660.A0A1G4IP83; -.
DR OrthoDB; 55978at2759; -.
DR Proteomes; UP000190274; Chromosome A.
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 CDD; cd12098; DD_R_ScPKA-like; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR11635:SF152; CAMP-DEPENDENT PROTEIN KINASE TYPE II REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
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 {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRNR:PIRNR000548};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566,
KW ECO:0000256|PIRNR:PIRNR000548};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000548,
KW ECO:0000256|PIRSR:PIRSR000548-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 227..342
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 345..452
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 95..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 301
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 411
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 420
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ SEQUENCE 461 AA; 51023 MW; 2AD4916E11F1A7B3 CRC64;
MPLSSGQLEE LNLFQRKVYE DEPKDLLQFA ANYFNRRLEQ QRFFARNQES VALSKGIVLF
PSATRNDSVV ASGRAGVAGL QSQSQDQLFK ASFSETTDPH GTRLHDPAPT ATDEAGHAQE
DTGFGSGIFK NDFRVNQSTE KNIKKPLDPM APAEEASGSS PQPSNTPRRS VVAPRPLPMN
FNAQRRTSVS GETMKPDNLD NWIPENYAEK SGLQLERLEK AIGHNFLFNK LDAESKRLVI
NSLEEKVVKN GQEIIKQGDE GDYFYVVEKG TVEFFVGSEK VNSSGPGSSF GELALMYNSP
RAATVVATTD CVLWALDRLT FRRILLGSSF KKRVLYDELL KSMPVLRSLT TYDRAKLADA
LDTEVYQPGQ IIIREGDIGE NFYFIEVGEA AVSKEGEGII AHLKKGDYFG EVALLNDLPR
QATVKAIKKT RVATLGKSGF QRLLGPAVEV LKLNDPTRVA H
//
