KAPR_COLTR
ID KAPR_COLTR Reviewed; 404 AA.
AC O42794;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR;
OS Colletotrichum trifolii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=5466;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10339807; DOI=10.1007/s002030050707;
RA Yang Z., Dickman M.B.;
RT "Molecular cloning and characterization of Ct-PKAR, a gene encoding the
RT regulatory subunit of cAMP-dependent protein kinase in Colletotrichum
RT trifolii.";
RL Arch. Microbiol. 171:249-256(1999).
CC -!- FUNCTION: cAMP-dependent protein kinase PKA regulatory subunit.
CC {ECO:0000269|PubMed:10339807}.
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; AF046922; AAC04356.1; -; Genomic_DNA.
DR AlphaFoldDB; O42794; -.
DR SMR; O42794; -.
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; 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..404
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205406"
FT REGION 14..144
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT BINDING 145..276
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 223
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 277..398
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 344
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 44778 MW; 4A60317816E3FF04 CRC64;
MAFPTYRPVQ CSKLTDHELL RIPHSPSLEP LDYCIEPISY LRRTVYDLHT TVANRSSSRA
LLHKQPPVMF KSPFGANANP FGGASDGATV GGNAMHQYNF SRRTSVSAES LKPSADTYDN
WTPPVHDKTN EQLSRLKTAI AGNFLFSHLD DEQSAQILGA LIEKPIPAKD IKVISQGDAG
EYFYVVEKGS FDVYVNEKGT LQPGPEGMGE KVGTIQAGGS FGELALMYNA PRAATVISAE
PGCTLWALDR LTFRRILMES TFLAAACTRT SSEKFPCCRH SHHMSAQKSP TRWKLRSTPL
VRRLSRRETR VTRFTCSRWR GRCLPGEMAR ESVKHYSKGD FFGELALLND APRAASIVAT
TDVKVASLGK SAFQRLLGPV EGIMRRTKYD DIKTGVEEMD PLQV