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Database: UniProt
Entry: U9TAQ7_RHIID
LinkDB: U9TAQ7_RHIID
Original site: U9TAQ7_RHIID 
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
//
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