ID Q8I6Y7_ONCVO Unreviewed; 373 AA.
AC Q8I6Y7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=cAMP-dependent protein kinase {ECO:0000313|EMBL:AAN78131.1, ECO:0000313|EnsemblMetazoa:OVOC4935.1};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000313|EMBL:AAN78131.1};
RN [1] {ECO:0000313|EMBL:AAN78131.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12706794; DOI=10.1016/S0166-6851(03)00041-0;
RA Fischer P., Djoha S., Buttner D.W., Zipfel P.F.;
RT "Isolation and characterization of the regulatory subunit of cAMP-dependent
RT protein kinase from the filarial parasite Onchocerca volvulus.";
RL Mol. Biochem. Parasitol. 128:33-42(2003).
RN [2] {ECO:0000313|Proteomes:UP000024404}
RP NUCLEOTIDE SEQUENCE.
RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA Berriman M.;
RT "Genome sequencing of Onchocerca volvulus.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:OVOC4935.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753}.
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DR EMBL; CMVM020000146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY159364; AAN78131.1; -; mRNA.
DR AlphaFoldDB; Q8I6Y7; -.
DR STRING; 6282.Q8I6Y7; -.
DR EnsemblMetazoa; OVOC4935.1; OVOC4935.1; WBGene00241744.
DR EnsemblMetazoa; OVOC4935.2; OVOC4935.2; WBGene00241744.
DR HOGENOM; CLU_018310_1_0_1; -.
DR OMA; DQWERAN; -.
DR Proteomes; UP000024404; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-BETA 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 2: Evidence at transcript level;
KW cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW 1}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000313|EMBL:AAN78131.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000024404};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AAN78131.1}.
FT DOMAIN 128..244
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 247..368
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 58..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
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 202
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 318
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 327
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 373 AA; 42072 MW; E84B2656C394815B CRC64;
MASGDSSEEA QLAQCQAYVQ RHNIQQLVKE AIVSLCINKP ENPVLFLKEH FEKLYDQRSQ
VSSPRIEATD DDDTIDEPPK LQQGNRRRLA VSAEVPDENE AANYDKVVIP KDDETRRALE
AAMCKNILFS HLEGDEQKAI FDAMFPVEKK KGETIIEQGE EGDNFYVIDS GEVDVFVNGE
YALSIKEGGS FGELALIYGT PRAATVVAKS DVVKCWAIDR ITYRQILMGS TMRKRKLYDE
FLSKVQILSD LDKWERANVA DALERCDFEP GTHVVEQGHP GDEFFIIVEG QADVLQKRSD
DAPFEIVGHL SSSDYFGEIA LLLDRPRAAT VIAKTPLKCV KLDRARFERV MGPVREILKR
DVSNYNSYVK LMT
//
