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Database: UniProt
Entry: K8F236_9CHLO
LinkDB: K8F236_9CHLO
Original site: K8F236_9CHLO 
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
//
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