ID Q2JFA8_FRACC Unreviewed; 548 AA. AC Q2JFA8; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 113. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABD10034.1}; GN OrderedLocusNames=Francci3_0650 {ECO:0000313|EMBL:ABD10034.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD10034.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD10034.1, 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; ABD10034.1; -; Genomic_DNA. DR RefSeq; WP_011435103.1; NZ_JENI01000019.1. DR AlphaFoldDB; Q2JFA8; -. DR STRING; 106370.Francci3_0650; -. DR KEGG; fra:Francci3_0650; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_459108_0_0_11; -. DR OrthoDB; 9801841at2; -. DR PhylomeDB; Q2JFA8; -. 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; IPR025241; DUF4190. 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; PF13828; DUF4190; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01217; PRICHEXTENSN. 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:ABD10034.1}; 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:ABD10034.1}; KW Transferase {ECO:0000313|EMBL:ABD10034.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 482..508 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 520..545 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 16..270 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 298..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 383..468 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 383..397 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..454 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 548 AA; 57007 MW; F4248D1D279CB844 CRC64; MLTPLMEEDP RQIGPYRLQN RIGAGGMGTV YLGFAPDRRP VAVKVAAEDL AEDEEFRSRF EREVRAALRV RGTAVAAVLD ADTEAAAPWM VTEYVEGTSL AEAVRARGRL EDHLVRGLAV GLADALVAIH AAGVVHRDLK PSNILLAWDG PKVIDFGIAH LTDSATLTRT GHVIGTLAWM SPEQMRGEPS DASADVFAWA SCVTYAATGR HPFHAETPDL LAVRVQRDSP DLYALPGYLL NQVARALSKA PRERPDAASL LAALVGREVR GVTEADAAAG DVLERTWTGS SPAFGVPAPF PAPVSSPSPN RSGPRVPGAG RVPARPAPGA AGSAGGWAPD VQGPGPAPGL WPVGPPPPAS AFRPAVPLPP AAPLRPVAPP AVAPPAVAPP AVAPPPSSGA VSPGGWADQA PAGRRGTTAA DVASDPGRSE VTYRSSDPTP PARPPDPSAF PPAGRPAAPR VGRWTDARRA EASRRRHWNS AAMLSVLLAV LWIFGIGSAA AVVVGLVARV RIRHRDERGA TVAAFGIGLG WLGIGLTMIL IVVILKFV //