ID A0A183QEY2_9TREM Unreviewed; 376 AA.
AC A0A183QEY2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000218901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000218901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753}.
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DR AlphaFoldDB; A0A183QEY2; -.
DR STRING; 6188.A0A183QEY2; -.
DR WBParaSite; SROB_0000218901-mRNA-1; SROB_0000218901-mRNA-1; SROB_0000218901.
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; cd12099; DD_RII_PKA; 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|PIRSR:PIRSR000548-1};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW 1}; Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 117..236
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 239..360
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 48..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
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 195
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 310
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 319
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 376 AA; 42795 MW; 4732195EE5E7B569 CRC64;
MTMKDEVVVP PGLRELLQEL TVSILREHPD NLIQFAIDFL MMKKAASENR QNKTNESEDE
DEEPMPIPPQ RATRRAGVAA ESYDPEKDDT SNVEKVVHPK TEEQRRRLAQ ATKDILLFRC
LDDDQMKDVI DAMYERHVSP GEKVITLGED GDNFYVIESG IYDIIVKVGN EEKTVGKYDN
KGSFGELALM YNTPRAATIL AKTEGVVWVM TREVFRSIVL KKAFEKRRLY EELLNQVPIL
ESLSAYERMS IADALRTKIF KDNQQIIRQG DPGDEMFFVE EGKVRIKMKR SGETEEKEVA
VIEKGGYFGE LALLTSHPRA ASAYADGQTK LAVLDVGSFE RLLGPCLDIL RRNIDDYEAK
LKNIFGSLDK VPELRR
//