ID A0A075A0S6_9TREM Unreviewed; 376 AA.
AC A0A075A0S6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cyclic nucleotide-binding domain protein {ECO:0000313|EMBL:OON13509.1};
GN ORFNames=T265_00812 {ECO:0000313|EMBL:KER33313.1}, X801_10716
GN {ECO:0000313|EMBL:OON13509.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER33313.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER33313.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OON13509.1, ECO:0000313|Proteomes:UP000243686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Khon Kaen {ECO:0000313|EMBL:OON13509.1};
RA Mitreva M.;
RT "Draft genome of the nematode, Opisthorchis viverrini.";
RL Submitted (MAR-2015) 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; KL596626; KER33313.1; -; Genomic_DNA.
DR EMBL; KV907355; OON13509.1; -; Genomic_DNA.
DR RefSeq; XP_009162948.1; XM_009164684.1.
DR AlphaFoldDB; A0A075A0S6; -.
DR STRING; 6198.A0A075A0S6; -.
DR GeneID; 20315000; -.
DR KEGG; ovi:T265_00812; -.
DR CTD; 20315000; -.
DR OrthoDB; 55978at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR Proteomes; UP000243686; 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; cd12100; DD_CABYR_SP17; 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; IPR047579; DD_CABYR_SP17.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 122..241
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 244..366
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 53..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
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 200
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 316
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 325
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; 42982 MW; 2A89327B98A6346A CRC64;
MEGKKKLPRI PPGFQELLES LSYDVLRAQP DDVLRFCIEN LNNRLSIVQE EGTQKAEFTD
NDNSLPITQS DAPPPRKARE RRGGVAAESW DPENVENTEK VVYPKTEEQK SSLLEAVRQI
LLFRCLDEDD RLDVVDAMFQ RTVEPEEDVI TYGEMGDNFY IIESGTYDIY VNINNEMKKV
TQYVDKGSFG ELALMYNTPR AATIRAVTPG VLWAMSRETF RSIVLTKAFK KRKLYESLLE
SVDLLKPLSQ YERNNLADAL YTRIVEEGES IFLQGDVGQE MFFIESGSVV VRMTTPEKPD
EYTELCTLGQ YQYFGELALL TKNPRAASVY ALERTRLAVL EVDSFERILG PCQDLLKQKA
QEYAETLDKL TAENRL
//
