ID Q0RSN4_FRAAA Unreviewed; 617 AA. AC Q0RSN4; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011}; GN OrderedLocusNames=FRAAL0755 {ECO:0000313|EMBL:CAJ59425.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59425.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ59425.1, 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; CAJ59425.1; -; Genomic_DNA. DR RefSeq; WP_011601994.1; NC_008278.1. DR AlphaFoldDB; Q0RSN4; -. DR STRING; 326424.FRAAL0755; -. DR KEGG; fal:FRAAL0755; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_1_11; -. DR OrthoDB; 3915799at2; -. DR Proteomes; UP000000657; 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-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 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; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01217; PRICHEXTENSN. 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}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Transferase {ECO:0000313|EMBL:CAJ59425.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 454..476 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 483..502 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 508..527 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 539..558 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 16..268 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 265..448 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 565..617 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..315 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..343 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..425 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 617 AA; 63364 MW; 1171E0D94DC65A72 CRC64; MLRPLTDTDP RIMGPYRLHY RIGAGGMGVV YLGFADEDRP VAVKVPHEAY ASDPEFRARF RSEVTAARHV QASTVARVIN AEVEGSRPWL ATEYVPGPTL HAAVLEHGPL VDRHLDNLTI GLAAALEAIH DAGVVHRDLK PANIVMSWTG PKVIDFGVAR SAEYTGYTQA GELVGTIAWM SPEQLDGQIA GPAADIFAWA CCVVFAATGR RPFRGETQEI VALRIGAAEP DLDGTPDRLL DAVSRCLAKD PARRPAAGEL VRLLSRRFSQ PATPGDERTP PDPPTITPPP PDPPPPDPPI IDPPPITPLT IETPKPDPRG PGAQDAENRD RNPESRGPVP EDHDVTRLAP PGPPPTPPPT PSRPTPPRPT PPSPTPSRPT PPSPTSPRPT PSRPTPSPPP LPSPPTPSPP PVPSPPAPLP PPVPAGAADD ERAEGDLPVP PAAPTVVRPP SLPLGMLVVL LTAGGLVGAV GIWAAGTARA GHAVLGPAAA TVTGAVCAQL LFLSNRAIGA AVTVLAAFVG SGGGVLLARS LDVGEPGRVL LCVAVALVVA ATGAFAMLPP RPATTGARPE LAADPAAGPA AAGPAAAGPA AAGPARDPRA PGQDADDAGR SLLRPAP //