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Database: UniProt
Entry: A0A158RDF9_HYDTA
LinkDB: A0A158RDF9_HYDTA
Original site: A0A158RDF9_HYDTA 
ID   A0A158RDF9_HYDTA        Unreviewed;       478 AA.
AC   A0A158RDF9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit {ECO:0000313|WBParaSite:TTAC_0000055001-mRNA-1};
GN   ORFNames=TTAC_LOCUS551 {ECO:0000313|EMBL:VDM16629.1};
OS   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000055001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000055001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM16629.1, ECO:0000313|Proteomes:UP000274429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   EMBL; UYWX01000053; VDM16629.1; -; Genomic_DNA.
DR   STRING; 6205.A0A158RDF9; -.
DR   WBParaSite; TTAC_0000055001-mRNA-1; TTAC_0000055001-mRNA-1; TTAC_0000055001.
DR   Proteomes; UP000046396; Unplaced.
DR   Proteomes; UP000274429; Unassembled WGS sequence.
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; cd12097; DD_RI_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:SF129; CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 2.
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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
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   Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          205..321
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          352..473
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          51..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270
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         279
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         423
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         432
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   478 AA;  53110 MW;  4FE54170685A5223 CRC64;
     MEDDLYAQEL DDYVKRHNIH KILRESIVNV CLYRPDDPIR FLREYFEALD TSSSHTEPAS
     NRSSNSAVPV GKRILGSRDG NASFPPPSAD SEPSSNPDNI PLDEPSTSAQ RRHSGDHYSS
     NQNGLSDVDD AYGSSGEVHF LSSSTSSTVN CSSSNPISAK RRVRRGAVSG EVYTEEDAAS
     YVKKVVPKDY KTMTALSKAI ARNVLFAHLD ENERSDIFDA MFPLHRSRGD IIIKQGDDGD
     NFYIIDQGKV DIYVNGELVS CIGEGGSFGE LALIYGTPRA ATVKARSDEV KLWGIDRDSY
     RRILMGSTIR RRKMYQDFLA RVPILGKRNP NNQASISSLS SCMLTVRLRF PLVDNLEKWE
     RLTVADALEP VRFEAGDCIV QQGDPGDDFY IIIEGTAAVL QRPSENSEPV EVGRLGPSDY
     FGEVALLLDR PRAATVVAQS AMRCVKLDRK RFERVMGPCS DILKRNIAKY NSYISLSV
//
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