ID Q0RRK1_FRAAA Unreviewed; 680 AA. AC Q0RRK1; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CAJ59817.1}; DE EC=2.7.11.1 {ECO:0000313|EMBL:CAJ59817.1}; GN OrderedLocusNames=FRAAL1155 {ECO:0000313|EMBL:CAJ59817.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59817.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ59817.1, 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; CAJ59817.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RRK1; -. DR STRING; 326424.FRAAL1155; -. DR KEGG; fal:FRAAL1155; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_459108_0_0_11; -. 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: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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR025241; DUF4190. 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; PF13828; DUF4190; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAJ59817.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAJ59817.1}; KW Transferase {ECO:0000313|EMBL:CAJ59817.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 614..642 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 654..679 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 38..305 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 324..601 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..445 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 460..494 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 517..547 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..562 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 680 AA; 70449 MW; 00AC1087A70860B1 CRC64; MGGCPHHTRE ISSREISGVR RGMLTPLLED DPRQIGPYRL QNRIGAGGMG TVYLGFTPEQ HPVAVKVAAE ELAEDVEFRS RFEREVHAAL RVRGNAVAAV LDADTEAPAP WMVTEYVEGI SLAEAVRARG RLENHLVRGL AVGLADALVA IHAAGVVHRD LKPSNILLAW DGPKVIDFGV AHISDSSTLT RTGHVIGTLA WMSPEQMRGD ASDSSADIFA WASCVTYAAT GRHPFHAETP DKLALRVQRD TPDLDALPAY LLTSVAGALS KIPRQRPTAS ALLASLVGRE VQGVTEADAV AGDFLERTWT GTARAASDGL TVLPAGEWSG ADRARAADGP EGDGRSDPAP SGGGRPSAAG GWSPSVQGPP PASGPWPVGP PPPASAFRPA VSPPPTIPPP PPLPASRLTP LPPAPLPPSA PPPSTPPAPR PSAARVPPGA SPPAGSQPVV SPWTYDMDEP DSRAPVRPRR EPPPDPHAAG ETRPRSRTDQ AEDTIRPPDP TPPARPPDPS EFQVWIRPAS AASSSAPSSS APPLSRRVSS SPSSSRAPTR PTPAPLPASP PRRSAAAAPG GIAAASGGRG HRIPVAVGGG GGEGSDARRF PPTTPVEHGL NGRALLSVVL ALGWLFGVGS VAAIVVGSMA QAQIRRHNQR GRRLAAVGIA LGWTGIGLTV VSLLIVLALR //