ID Q3SEN6_PARTE Unreviewed; 807 AA.
AC Q3SEN6;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00024113};
GN Name=pkg5-4 {ECO:0000313|EMBL:CAH69649.1};
GN ORFNames=GSPATT00000934001 {ECO:0000313|EMBL:CAK71221.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAH69649.1};
RN [1] {ECO:0000313|EMBL:CAH69649.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAH69649.1}
RP NUCLEOTIDE SEQUENCE.
RA Kissmehl R., Krueger T., Treptau T., Froissard M., Plattner H.;
RT "Identification of a multigene family encoding cGMP-dependent protein
RT kinases in Paramecium tetraurelia cells.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAK71221.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK71221.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [4] {ECO:0000313|EMBL:CAK71221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK71221.1};
RG Genoscope;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CR855944; CAH69649.1; -; Genomic_DNA.
DR EMBL; CT868096; CAK71221.1; -; Genomic_DNA.
DR RefSeq; XP_001438618.1; XM_001438581.1.
DR AlphaFoldDB; Q3SEN6; -.
DR STRING; 5888.Q3SEN6; -.
DR EnsemblProtists; CAK71221; CAK71221; GSPATT00000934001.
DR GeneID; 5024403; -.
DR KEGG; ptm:GSPATT00000934001; -.
DR eggNOG; KOG0614; Eukaryota.
DR HOGENOM; CLU_000288_73_2_1; -.
DR InParanoid; Q3SEN6; -.
DR OMA; GTPECMA; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF153; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000313|EMBL:CAH69649.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..224
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 227..327
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 348..446
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 481..738
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 807 AA; 92530 MW; C6B1B4504A0E038F CRC64;
MGNICRQSPI NDKNDIEVNT SQPPPIQQVH PPKPDEVKTQ APEKQEEPAQ SIDQAKQENE
PKRKEQKKMG KIAAVIDQEV IYENVQKQEK VKSPFDFQLL LNAFGNSFIF GQLQPEDKVK
VIDKMFYCTV HDGEMVFKQG DKASSYFLIE RGQCQIIINN ELKKTLKSGE AFGELALLYN
APRSATVKAV GDCAFWAIDR NTVRKAIESI SQKDYDQNKE FINKVPFFES LTDDQKAAIP
SALINLNFKA GEIIVNEGDQ ADSFFIIKKG EIQISRGGKE LRIMRAGDSL GEQALQQNSV
RGATAKAIKE DATVLALARD DLTRILGDKI QLIMYSNLQR WAFERHVVLS KLTKLQVERI
VSNMQQTQKK SEEVIIEKGQ ACREIIIVLQ GSVRYGKEIL EKGQMFGDKF LDQGENVKLG
EPVVMKDEGM IATITFKQFF EIIGGSLEQI FAKNEKAHDR FIKKEEGQKQ DVFKHFQLDQ
LIHVKKLGQG QFGNVYLVHN KMDKKIYALK CISKAQIIEQ NLEKHLAQEK IALETVNFPL
IMHFARSFRD TTYIYFLEEY IRGMELFDVI RDIGLLNTYD SQFYIGSLIL CMEYLHLNNI
IYRDIKPENI MIDEKGFMKL IDLGTAKNLK SKNGRTYTII GTPHYMAPEI LTGKGYTYSV
DLWSIGICLY EFMCGNVPYA EDADDPYEIY EEIQKKQLTF PSVLKDRKAK KLIEQLLSKT
PELRLGSSYA SLKNNTFFER FDYDLLINRE LKPPYLPPKN KLHSEKDIQK AIQVGKLVTE
EIKNDLATAQ NVYKPEKARD PNWDKDY
//
