ID Q2JB34_FRACC Unreviewed; 660 AA. AC Q2JB34; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 123. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN OrderedLocusNames=Francci3_2136 {ECO:0000313|EMBL:ABD11508.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales; OC Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD11508.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD11508.1, 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; ABD11508.1; -; Genomic_DNA. DR RefSeq; WP_011436555.1; NC_007777.1. DR AlphaFoldDB; Q2JB34; -. DR STRING; 106370.Francci3_2136; -. DR KEGG; fra:Francci3_2136; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000001937; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; 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:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}. FT DOMAIN 13..281 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 282..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 286..307 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..428 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 429..442 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 142 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 660 AA; 67622 MW; AD6978EB6AA89FD0 CRC64; MVGHAGLVVA GRYRLQDRLG AGGMGAVWRA TDQMLRVDVA LKEVSIPVDS TPGEWTERIA RARREGMNAA RLRGHPGIVS VHDVVEDGGL PWIVMDLIIP ARSVADRLRG SGGLRPDETA SIGAAVADAL AFAHAKGVVH RDIKPGNILL AESGRALVTD FGIAAHNDDS RMTAAGVVGT IAYVAPERLG GQPADGRSDV FSLGVTLYQM VEGRLPFQAD TTAGLLSAIL FEPPRPTVLA GPLRPVLDAM LEKDPVVRLD AAAAARALAS LAAGGPASPV LVPAQVPTPT PAQLPPPAQV PTPPLPRVPT VSRPATALLP PVGEPEAGGS RWPDSGMPGT PGLSGAPGRP SGRVWLVAGT LTAVLAILAG VFLARGGVGA HPGDGSLTGT ASATVAATGP EDGVPRVSPS AAASGAGSGA ASGAGTSAGT GARTSSATAA GSPRPSQELT VVPSFSAAAP GVSQYSADYY ATLTRSRQDG FLLRVGFDAT GRSDLRDPRT SCVLVSSGSR ELRLFPVQAD VPVSSSGRYS GTLTFSLALP GSYRFRYSCQ ADYSAALLGT VTMPSVAVSV YDDNYFVNVL EVRVGAGRTV VFFAAAGAAD LRVPVTSCLR LESGIRRPVV ELKTSRKSPT GATYIGTMRF EGTPPATLVY SCSDYSPVNL //