ID G2Y2J4_BOTF4 Unreviewed; 468 AA.
AC G2Y2J4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit {ECO:0000256|ARBA:ARBA00020355, ECO:0000256|PIRNR:PIRNR000548};
GN ORFNames=BofuT4P313000020001 {ECO:0000313|EMBL:CCD46884.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD46884.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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|ARBA:ARBA00025979,
CC ECO:0000256|PIRNR:PIRNR000548}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753, ECO:0000256|PIRNR:PIRNR000548}.
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; FQ790283; CCD46884.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y2J4; -.
DR STRING; 999810.G2Y2J4; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; G2Y2J4; -.
DR Proteomes; UP000008177; Unplaced contigs.
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; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 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:UP000008177};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 212..341
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 344..461
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 139..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
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 299
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 468 AA; 50778 MW; EBCB39F484D7852E CRC64;
MSLPSVYLTE IESLSQEILR NQPTDILQFC ANYFSQRLET ERAGFLTSRN RSYRSVSPGT
ANRPRMAGNT FPGRLGTHAN PFGGDGNGLG HEQAVPGNIS KVIEEDENDT ITSPTTPNFG
FSKGVPSFGA SFGPSFGGSF GGDASTGDFP PSSFKPASEG FPEHYGMGRR TSVSAESLNP
TASSNDNWSP PFHQKTQDQV ARLKKSISGN FLFSHLDDEQ SAQVLGALVE KPIPAVGIKV
ISQGDQGDFF YVVEKGSFDV HVNSTGSLQP GPDGLGTKVA TIEPGGSFGE LALMYNAPRA
ATVISAEASC TLWALDRITF RRILMDSTFQ RRRLYESFLE EVPLLSTLTR YERSKIADAL
ETQKYPPGTA IINEGDAGEA FYLLESGEAE AYKRGVDNPV KLYHKGDYFG ELALLNDAPR
AASVVSKTEV KVATLGKNGF QRLLGPVESI MRRTKYESVE SIDPLHQN
//
