ID Q2J7G9_FRACC Unreviewed; 898 AA. AC Q2J7G9; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 124. DE SubName: Full=Serine/threonine protein kinase with WD40 repeats {ECO:0000313|EMBL:ABD12773.1}; GN OrderedLocusNames=Francci3_3419 {ECO:0000313|EMBL:ABD12773.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD12773.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD12773.1, 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; ABD12773.1; -; Genomic_DNA. DR RefSeq; WP_011437798.1; NZ_JENI01000031.1. DR AlphaFoldDB; Q2J7G9; -. DR STRING; 106370.Francci3_3419; -. DR KEGG; fra:Francci3_3419; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2319; Bacteria. DR HOGENOM; CLU_000288_135_4_11; -. DR OrthoDB; 3217714at2; -. DR PhylomeDB; Q2J7G9; -. 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 CDD; cd00200; WD40; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. 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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR22847:SF748; TRANSCRIPTIONAL REPRESSOR TUP11; 1. DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 5. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABD12773.1}; 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:ABD12773.1}; KW Transferase {ECO:0000313|EMBL:ABD12773.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE- KW ProRule:PRU00221}. FT TRANSMEM 474..494 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 28..281 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 559..592 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 612..646 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 650..691 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 695..736 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 740..774 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 829..870 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 304..410 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 422..468 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..343 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 375..392 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 898 AA; 92746 MW; 0292197AC8DF48FC CRC64; MSHPPGRSGP ADGPADRAAS EPTEVGPYRL VRRLGAGGMG TVYLGENAAG GLVAVKLIRA DLARLAEFRS RLKQEADNAR RVARFCTAAV LDVDITADPP YLVTEYVDGP TLSEAVGTRG PLTPAELHQL AVSMTTALMA IHRAGLVHRD LKPSNILLSR LGPKVIDFGI ARALDSATVL SGDRQLGTPA FMAPEQALGE QVTSAADVFA WGGVLIFAGT GRYPFGNGPA PSVLYRTVND PPTLDGFEDS LRPLVSDAMR KAAAERPTAE KLYARLLDLR VEAPMAVKGL SLSEVTALIR PLNTSPGGAS GTSASDADLA GPITPVTGHQ PIGPPPPANL ISFPGPGIPG APARSGPSSV PGPSSVPGPS SVPGPTSSPG LGSSSSGSEA SPSGPDARWL PGAGSSSRSR DFADALVTVW TEDEHSQDPG RGASPSSSSS SSQRSSSSQR SSSSSRRSSS AAPPGDRARN RRPLIIVALV AAVTVLVTTV AIVSTRGGGS RTEMSVPEAV AERALLLQDG DTGLARRLAL AAYRAEPHSA RTRSAMIALF GAGITPTTIP VGTGALLALA VSPDGHWIAA GSNNGTVTLW EVVGRTELVR RTSVSVPSRS WIESLAFNRD GGLLAAGHSD GTIRLWNLHD PDQMVRWSTI QAHTDAVQSV AFSPDSNTLG SASADGIVAL WDVTDPARPK QRVRADGQTG GVRSMAFAPN GTLLAFAGED GTVHLWNIRD AARPTAGGIL RGHSRGVRSV VFTGDGGVLV SGGVDATVRL WEVRYPDNPA RGVATGSLGG IQSVAFEPGA DVVASAGDDE TVRLTDISRL DTPILLTQWH GHTQPISAIA FVSGTGVVVS AGHDGTLRLW DAEPGRLADT ACADPANRIT AGEWSTAFRD MGYRAPCG //