ID Q0RGS3_FRAAA Unreviewed; 730 AA. AC Q0RGS3; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 104. DE SubName: Full=Putative eukaryotic-type serine/threonine protein kinase {ECO:0000313|EMBL:CAJ63313.1}; DE EC=2.7.1.- {ECO:0000313|EMBL:CAJ63313.1}; GN OrderedLocusNames=FRAAL4671 {ECO:0000313|EMBL:CAJ63313.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63313.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ63313.1, ECO:0000313|Proteomes:UP000000657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657}; 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; CT573213; CAJ63313.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RGS3; -. DR STRING; 326424.FRAAL4671; -. DR KEGG; fal:FRAAL4671; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3386; Bacteria. DR HOGENOM; CLU_383001_0_0_11; -. DR Proteomes; UP000000657; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. 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; 2.120.10.30; TolB, C-terminal domain; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR001258; NHL_repeat. 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; PF01436; NHL; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF101898; NHL repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51125; NHL; 2. 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:CAJ63313.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAJ63313.1}; KW Transferase {ECO:0000313|EMBL:CAJ63313.1}. FT DOMAIN 40..294 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 395..427 FT /note="NHL" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504" FT REPEAT 679..722 FT /note="NHL" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504" FT REGION 367..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 367..381 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 69 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 730 AA; 74737 MW; 226C1865CAFF1ABA CRC64; MAAWLGLLAC DTDFRSGAAG PLPPDMIIDR RRVQKALPGY ALGAELGSGA FGLVLAGKHR RLGRPVAIKV MQAEGPEGRS LDFAAEARVL AGFDHPHVVK AYDYVEAEGL CLVVMELLAG GTLSRRRAGM TPQAGCAVGL AVAAALEHAH SFGVLHRDIK GDNILFTADG IAKVTDFGIA KLLEGSGATA SSRSGTPMYM APEQIDGGRL GPATDLYALG VVMYQLLTGA PPFDPRQSVS RLWRQHLTDP PPPMIDVPAP LAAVVLRALA KKSADRQPDA RTFALELAAA AATVYGPGWA GIPLRLDADI RSTANLMPAP IRPPSGMASR HRSSPAVGRT RFRPRWVVAV ALAALAATST LVALRSNNGS SPTSSGTFNT PTPTPAPGPA AVAVGPLSRP AGVAVGGDGS VYIADIEEHR VWKVDRAGRM STLAGTGTAG FSGDGGPANR AQVNWVAALA VGADSSVYMV DSNLDLDESR IRKIDGAGRI STIAGNGRAV DLGESGSSGD GGPALDSPLS GVGALAVGAD GVVYLADEAS NRIRRVDRAG LISTFAGAGT SPSPSRFFGD GGPATRAQLD CGNACGVAVG ADGSVYIADE GNNRIRKVDQ AGRISTIAGN GSLGFAGDGG LAIQAQMMYP LQVAVGPDSS VYILDDANDV RKVDPSGRIT LFAGNGTGGF SGDGGPATRA QMNQPSAIAV GSDGSVYIAD EGNKRIRKID PAGRINTIAR //