ID U9TAQ7_RHIID Unreviewed; 339 AA.
AC U9TAQ7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit {ECO:0000256|ARBA:ARBA00020355, ECO:0000256|PIRNR:PIRNR000548};
GN ORFNames=GLOINDRAFT_82862 {ECO:0000313|EMBL:ESA05230.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA05230.1};
RN [1] {ECO:0000313|EMBL:ESA05230.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA05230.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) 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; KI293301; ESA05230.1; -; Genomic_DNA.
DR AlphaFoldDB; U9TAQ7; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_1_1_1; -.
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; Jelly Rolls; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
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 I REGULATORY SUBUNIT-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
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}.
FT DOMAIN 55..170
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 173..293
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
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 129
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 243
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 252
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 339 AA; 37989 MW; 9E068002EA7DCE8C CRC64;
MRNNQTRVIT PRKGRRMSVS AESMRPSENV DERTIIYKSD EAKKRIDEAT TLNLLFKNLD
RETKQHVVDA MFEKSVVANE IVIKQGDEGD YFYVIEHGLF EIFVNGQLVL EIGDGGSFGE
LALMYNTPRA ATVRAKTNGT LWAVGRETFL RTITNSVYRK RKAYEDFLRS VSFLSTLDRS
EITKLADALE PNNYDDGDTI ISQGEPGEHF YIIEQGTVSI SKISDTGIEQ QLPSLNVGSY
FGELALINDQ PRKATVVARG SVRVAALRRD AFVRLLGPVM DIFRRNAAEY NLQQGRPQES
SDNHVSSQIN GDESMAVDIE DEYPRRRSGY SGAGGVDVL
//