ID Q2J4M1_FRACC Unreviewed; 613 AA. AC Q2J4M1; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=Francci3_4425 {ECO:0000313|EMBL:ABD13771.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD13771.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD13771.1, 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 --------------------------------------------------------------------------- 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; ABD13771.1; -; Genomic_DNA. DR AlphaFoldDB; Q2J4M1; -. DR STRING; 106370.Francci3_4425; -. DR KEGG; fra:Francci3_4425; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_1_11; -. DR PhylomeDB; Q2J4M1; -. 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; 2.60.40.1240; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR029051; DUF4352. DR InterPro; IPR029050; Immunoprotect_excell_Ig-like. 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; PF11611; DUF4352; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABD13771.1}; 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:ABD13771.1}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transferase {ECO:0000313|EMBL:ABD13771.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 432..452 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 43..296 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 15..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..422 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 455..491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 407..421 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..482 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 613 AA; 63898 MW; DF0B170E38B2CAE9 CRC64; MDSGRDHSRA VLTVADNAAR MGPGRSEPGD PLNPHEPRSV GPYVLLSRLG VGGMGTVYLA RNRAGRRVAI KVIRPDLAAD EEFRRRFRAE VEAARKVAPF CTAEVLDADP NAPAPYLVTE FIDGVRLDMQ VDKGPLTSST LTGLAVGVAT ALTAIHSAGL VHRDLKPSNV MLSLSGPRVI DFGIAQALEG AKAKPTAWGF GSAGWMAPEQ VHGQPIGPEA DVFAWGILIA YAGTGRHPFG DGTDIDLGMR IVGSAPDLRG LPQPLVGLVS AALAKHPDDR PSARDLLLRL IAQPPSRGTG AIGEAMGQAE ELLSRTGEVP RAAPTRIGPA TSAPARQVHW NAGAPAARAG QGPGQPRQAP PGQSGAHSPR GRPGPRPAQL GERMGGQVPG APPGPWSGQA PDRHGPVPGE PGAPYPSFAQ PPPARGLDRR RLVWIAVIVL GALIAIAVVV SLPGKSGQNG SAEQSAATTV PSRSTGPSTA PGPASGLNRP VTDGQLEFIV DSFRCGQTKL GDGLLARHTD GQFCLAHVTV RNIGDSTRTL VTSSQFLWDG GGGRHSADFL ARFQLSNEDL WDSINPGDLR AGTMVFDIPR DATAQELELH DNPVSAGARV PVP //