ID Q2JG45_FRACC Unreviewed; 508 AA. AC Q2JG45; A0A1X1Q2C0; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 111. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABD09747.1}; GN OrderedLocusNames=Francci3_0360 {ECO:0000313|EMBL:ABD09747.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD09747.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD09747.1, ECO:0000313|Proteomes:UP000001937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45818 / CECT 9043 / CcI3 RC {ECO:0000313|Proteomes:UP000001937}; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C., RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., RA Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00001433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000249; ABD09747.1; -; Genomic_DNA. DR RefSeq; WP_011434825.1; NZ_MSEA01000019.1. DR STRING; 106370.Francci3_0360; -. DR KEGG; fra:Francci3_0360; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_1_11; -. DR OrthoDB; 3915799at2; -. DR Proteomes; UP000001937; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABD09747.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001937}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABD09747.1}; KW Transferase {ECO:0000313|EMBL:ABD09747.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337..356 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 362..382 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 389..408 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 420..439 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 270..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 439..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 294..329 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 508 AA; 52455 MW; DEA4BC6E7FBBD383 CRC64; MLRPLNDTDP RVMGPYRLHN RIGAGGMGVV YLGFGPDDQP VAVKVPHEVH ASDPEFRARF RSEVSAARHV RADTVARVIR AEVDGPKPWL ATEYVAGPTL RAAVQEGGPL TGRPLDGLAI GLAAALEAIH AASVVHRDLK PANIVMSWAG PKVIDFGVAR SADYTGYTQA GELVGTVVWM APEQINGQQA GSAADVFAWG CCVVFAATGR RPFRGEAPEI VALHISSTEP ELDGVPERLL GPVRQALTKN PGHRPSAGEL VRLLTQRLSP EETADASNDV PPVTGAEPNR EQTRPTPNPG PPATPPPTPS PVPTPSFPAV GPAHPSRPSP SSSRPSVLTA LLALTGLAAT VGVWAAETER TGHAVVGPVA AAIIGLICGQ MIFLSDRRIG VLTTVAAAVS GSGIGLLLAR VLDVDEPNRV LLSVAGALIV ATAFAGAMAP SRPAPGDRPG TDGPGEPVGS HRLLEPTHPV SRTNTGGEAG TDAAGATLRL HGAAAPGQHL VPERPDPS //