ID Q2JH04_FRACC Unreviewed; 863 AA. AC Q2JH04; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 117. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABD09438.1}; GN OrderedLocusNames=Francci3_0044 {ECO:0000313|EMBL:ABD09438.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD09438.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD09438.1, 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; ABD09438.1; -; Genomic_DNA. DR AlphaFoldDB; Q2JH04; -. DR STRING; 106370.Francci3_0044; -. DR KEGG; fra:Francci3_0044; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3391; Bacteria. DR HOGENOM; CLU_383001_0_0_11; -. 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; 2.120.10.30; TolB, C-terminal domain; 3. 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 InterPro; IPR013658; SGL. DR PANTHER; PTHR13833; -; 1. DR PANTHER; PTHR13833:SF71; NHL DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08450; SGL; 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; 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:ABD09438.1}; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABD09438.1}; KW Transferase {ECO:0000313|EMBL:ABD09438.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 490..511 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 57..320 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 817..853 FT /note="NHL" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 337..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..433 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 86 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 863 AA; 87289 MW; DB3A07C8B23602E1 CRC64; MGGQGRRITR NPTKGVIAGQ DGSRRTGGGT ADARRGSGRI WTLLIDKSRV EAALPGYSVE GDLGRGGYGL VLAGQHRLIG RKVAIKILLD TSDDPDLRTR FLSEARVLAE LDHPHIVRIH DYVEHEGTCL LVMELLSGGT LKQRMSSGPV SAETTCSIGL AAAAALATAH GHGVLHRDIK PDNIMFAGDG LLKVTDFGIA KIFDGAETTA SAILGTPRYM APEQIMGTRL FPSTDLYALA GVLYEMIANR PLFGRQMAVQ PLTHHHLTIM PEPLTMVPPP VSAVILRALA KDPSIRFADA ADFALELARA SSRAFGPTWL SRSDVKVRID DEIREAALAT STTPRPPAAG RPGFPGSPGA PGSPGFPGSP GAPGSPGFPG SPGAPGSPAG HPMGGYPPPG GPGWGGFPPG NTPPPRSTPP PRSTPPPRSL GPGYGGPDAP GGPGAPGGPG GQTYRPGPGG PVHGMAGVPP AATRQAGHQS SPNARNRTPL IIGAVAFVVI VAITVGIVAA VTNSGGGSRG GDRGGGTARL ATAYRGTALS VQGLSPYSVD VDPDGSLLVS SLATDRIQKI TPAGAVSDLA GTGAGGISGD GGPATAAQLD GPGSTARDKA GNIYIGDAKN NRIRKISPAG IITTIAGTGD AGYGGDGGPA TAAKINSAEK VTTGPDGSVY LSDYENHRIR KISPQGIITT YVGTGVAGYT GDGGPATAAK INGPNDLQMT DDGTLYFADL ASDTIQKVTP DGIITTVAGT GEGGFSGDGG PATRARLNVP SLTVGPDGRT LYLADYRNHR IRRVDPNGVI TTIAGTGGEG SGGDGGPATA AQFKNPSSVA VDGSGALYIA DNGNDRVRRI DPNGTITTVA QPG //