ID Q0RQD7_FRAAA Unreviewed; 770 AA. AC Q0RQD7; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 100. DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CAJ60239.1}; DE EC=2.7.1.- {ECO:0000313|EMBL:CAJ60239.1}; GN OrderedLocusNames=FRAAL1583 {ECO:0000313|EMBL:CAJ60239.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ60239.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ60239.1, 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; CAJ60239.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RQD7; -. DR STRING; 326424.FRAAL1583; -. DR KEGG; fal:FRAAL1583; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0823; Bacteria. DR HOGENOM; CLU_000288_135_1_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; 2. 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; IPR011659; PD40. 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; PF07676; PD40; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 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}; Kinase {ECO:0000313|EMBL:CAJ60239.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAJ60239.1}; KW Transferase {ECO:0000313|EMBL:CAJ60239.1}. FT DOMAIN 19..269 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 295..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 339..408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 439..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 439..469 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 770 AA; 78940 MW; 951531907DE8DDBE CRC64; MAARAVPLGP DDPRELGSYT LLGKLGQGGM GMVYLGRSEK GRLVAIKVIR TEAVGNPEFR ARFRLEAETA RRVARVCTAE VLDADPDAEW PYLVTEFIEG ETLARYVQRN GPLADANLEQ LAVGVAAALT AIHSAGIVHR DLKPANVILS PFGPRVIDFG IARAVDAGSG LTGDLQQLGT PAFMSPEQIE SQPISSAVDI WAWGGLVAFA ATGHYPFGDA SAQVLLYRAL HEEPRLDDVD PALRPIVWLA MRKDPATRPT AQQLMLRLLG DPSGTGPDAA AAVDPQDVTN VLQGWNLPAP SPAGPGTSGP TAGAVGTGPA ADVGGRGVAA AAAGAGTGAA AGYTADPDAP TRLPTGLGAP VPPRTAGDGT VAGQSPTRVG AEAGGPSWPG GPGGSGGAAS PPGGAGARGH RNRVPLLVGG GVVVVGAILA GILALTSGGS DGGNSAATGS SPRPAASAGA ASTGAPSAQP GAFTLPRSPE PLGRDTVVYA SNRNGNYDLF RGDVTGDGGL QNDKPLLTGP DNDMLPAISG DRKTVVFFKK GSPNTLQAIA ADGTGKPVQL FTSGPAANLT IANDARPSLS PDGEFLVVRS STDEKRDQNP GLYIVRLDGS SVRRLKTKPQ ATDPAWSPDG ERIAYWSNNA GGDRGFVVVI SVEPDAVAQP VINDKLTTDS DPVWSPNGDK IAFTREQNGD LEIFEMGSDG SDVRQLTHAR GDDQDPAFGP DGRIVFSGQR DPANPNARQL FVLNPNDPAA GDRQLTTLGG FNGHARWNAG //