KAPR_MAGO7
ID KAPR_MAGO7 Reviewed; 390 AA.
AC O14448; A4RIF5; G4MVD9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=SUM1; Synonyms=RPKA; ORFNames=MGG_07335;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LEU-211.
RC STRAIN=Guyane 11;
RX PubMed=9707535; DOI=10.2307/3870646;
RA Adachi K., Hamer J.E.;
RT "Divergent cAMP signaling pathways regulate growth and pathogenesis in the
RT rice blast fungus Magnaporthe grisea.";
RL Plant Cell 10:1361-1374(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RA Gilbert R.D., Dean R.A.;
RT "The cAMP-dependent protein kinase regulatory subunit gene from Magnaporthe
RT grisea.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; AF024633; AAC34140.1; -; Genomic_DNA.
DR EMBL; AF015753; AAB70215.1; -; Genomic_DNA.
DR EMBL; CM001232; EHA55765.1; -; Genomic_DNA.
DR RefSeq; XP_003715572.1; XM_003715524.1.
DR AlphaFoldDB; O14448; -.
DR SMR; O14448; -.
DR STRING; 318829.MGG_07335T0; -.
DR PRIDE; O14448; -.
DR EnsemblFungi; MGG_07335T0; MGG_07335T0; MGG_07335.
DR GeneID; 2683231; -.
DR KEGG; mgr:MGG_07335; -.
DR VEuPathDB; FungiDB:MGG_07335; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_0_1; -.
DR InParanoid; O14448; -.
DR OMA; YDNWSPP; -.
DR OrthoDB; 1047290at2759; -.
DR PHI-base; PHI:128; -.
DR PHI-base; PHI:6818; -.
DR Proteomes; UP000009058; Chromosome 2.
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 1: Evidence at protein level;
KW cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..390
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205411"
FT REGION 1..129
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..261
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 208
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 262..383
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 329
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MUTAGEN 211
FT /note="L->R: In SUM1-99; restores cAMP-stimulated
FT appressorium formation and growth morphogenesis to
FT adenylate cyclase-deficient mutants."
FT /evidence="ECO:0000269|PubMed:9707535"
SQ SEQUENCE 390 AA; 42271 MW; 1BA8BD8A21439A8F CRC64;
MSASGFTSPF GANSNPFGSP EERRGVAGSI QPVLEEEEAD GIGSEPISFK SPGFRAPFGG
GDANSEGPPS SRPQNPDGYP AQYNFARRTS VSAESLKPIA DSYDNWTPPF HPKSAEQLDR
LKKAIQGNFL FSHLDDEQSA QILGALVEKP IPAKDIKVIV QGDAGDYFYV VEKGKFSVHV
NSSGVMQAGT QGLGDHVGTI EAGGSFGELA LMYNAPRAAT VMSAEPNCVL WALDRVTFRR
ILMESTFSRR RMYENFLEEV PILSTLTAYE RSKIADALET QKYPPGTVVI KEGDPGEDFY
LLECGEAEAF KAGIDQPVKL YKKGDFFGEL ALLNDAPRAA SVVSKTEVKV AALGKSAFQR
LLGPVEPIMR RTRYDAIKTG VEEMDPLQAA
