ID K8F236_9CHLO Unreviewed; 780 AA.
AC K8F236;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Bathy07g03200 {ECO:0000313|EMBL:CCO66165.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO66165.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO66165.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO66165.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FO082272; CCO66165.1; -; Genomic_DNA.
DR RefSeq; XP_007512077.1; XM_007512015.1.
DR AlphaFoldDB; K8F236; -.
DR STRING; 41875.K8F236; -.
DR GeneID; 19014809; -.
DR KEGG; bpg:Bathy07g03200; -.
DR eggNOG; KOG0585; Eukaryota.
DR OrthoDB; 5475498at2759; -.
DR Proteomes; UP000198341; Chromosome_7.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14008; STKc_LKB1_CaMKK; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24346:SF77; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE KINASE 1; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 164..433
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 456..581
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 640..766
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 18..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT MOD_RES 695
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 780 AA; 87398 MW; 47B4CABB985847DB CRC64;
MSFFSSCFYC FAPKATETEE EKVLFDDDGD EISEKTNQVT LENVENEEND EKMNTDKTET
YEDNSRKDET NKNKNNKRNK DSERDKKKKT SGSANNNEEE NDRNSLSSNT GSSTSSTSST
NYNAQMKTPP QVANRRLGSL KLTPSVQKLS IIMDDKEHEQ LNQYIMIKDL GRGAHAKVKL
GLNKMDNNLY ALKIRNERVR VAEAAVRKEI AILKKLSHPH VLKLHEVIDD TVSNELILVL
EYAPGGPIFT RFNRVPLSEK VLHGYARDIV LGLDYLHSLE IAHMDLKPEN MLKMADGVKL
CDFGVSVDSE LTGVTRSTRL AGTPAFLAPE MLDETGYDPM PSDVWSLGVC LYNMATARLP
FTGKTVFQIV AMAKSTELKF PDEDADAIVN ATTVPSPPPP KLSNLLKDML RKMLVVDPKE
RISIAGMMEH PWVTEEGKKP LGRPRTKSPS MKLEVTEEDI DNAVRTNPLA AILQPAFRIE
RFKDGEVLMR KGEVGDRMYF INKGECEVLM DALLEAAAVV DDSSSKNNDN EDVLCIRYAG
EIVGELAFLT AIEKRKDKKT PGVGYRNATV RAKGEVECLA VTVTDMLEAL EFDESSRASV
VEVAEYRNRQ TEEVIQQIAE SKLDDAKHSK PVLNIEKTLR ILYAEDSLPT QMIVKALMRK
IGKVELTIAS NGREAVDVCK KLEKKEELFD LILMDCQMPV MDGLEATREI RKLENADGYF
ANIPIVAVSS GIISMTQDIC KEAGMDKYVM KPLSQKLLVD TLMNALEIHE EKKRSSESRD
//