KAPR_COLOR
ID KAPR_COLOR Reviewed; 391 AA.
AC Q9C1C2; A0A484G732; N4VDJ5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR; Synonyms=RPK1; ORFNames=Cob_09468, Cob_v000201;
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=11605954; DOI=10.1094/mpmi.2001.14.10.1149;
RA Takano Y., Komeda K., Kojima K., Okuno T.;
RT "Proper regulation of cyclic AMP-dependent protein kinase is required for
RT growth, conidiation, and appressorium function in the anthracnose fungus
RT Colletotrichum lagenarium.";
RL Mol. Plant Microbe Interact. 14:1149-1157(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=30893003; DOI=10.1094/mpmi-12-18-0352-a;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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; AF353397; AAK31209.1; -; Genomic_DNA.
DR EMBL; KB725947; ENH81822.1; -; Genomic_DNA.
DR EMBL; AMCV02000001; TDZ26072.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C1C2; -.
DR SMR; Q9C1C2; -.
DR STRING; 1213857.Q9C1C2; -.
DR EnsemblFungi; ENH81822; ENH81822; Cob_09468.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_0_1; -.
DR OrthoDB; 1047290at2759; -.
DR PHI-base; PHI:231; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
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; 2.
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..391
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205409"
FT REGION 1..131
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..261
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 210
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 264..381
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 331
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 42412 MW; E9EB6126C9B137E9 CRC64;
MFKSPFGANA NPFGGASDGA TVGGNAMHQV IEEEENDTVT SPTSPNFGMN AQSMFSGPFG
GDASDDVLPS ALRSPPNPES YPAQYNFSRR TSVSAESLKP SADTYDNWTP PVHDKTNEQL
SRLKTAIAGN FLFSHLDDEQ SAQILGALIE KPIPAKDIKV ISQGDAGDYF YVVEKGSFDV
YVNEKGTLQP GPEGMGEKVG TIQAGGSFGE LALMYNAPRA ATVISAEPGC TLWALDRLTF
RRILMESTFS RRRMYEDFLR EVPLLQTLTP YERSKIADAL ETQKYTPGAT IIKEGDPGHS
FYLLESGEAD AYLGDGKESV KHYSKGDFFG ELALLNDAPR AASIVATTDV KVASLGKSAF
QRLLGPVEGI MRRTKYDDIK TGVEEMDPLQ V
