ID Q0RTZ6_FRAAA Unreviewed; 611 AA. AC Q0RTZ6; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 112. DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CAJ58949.1}; DE EC=2.7.11.1 {ECO:0000313|EMBL:CAJ58949.1}; GN OrderedLocusNames=FRAAL0272 {ECO:0000313|EMBL:CAJ58949.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ58949.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ58949.1, 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; CAJ58949.1; -; Genomic_DNA. DR RefSeq; WP_011601532.1; NC_008278.1. DR AlphaFoldDB; Q0RTZ6; -. DR STRING; 326424.FRAAL0272; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR KEGG; fal:FRAAL0272; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_446722_0_0_11; -. DR OrthoDB; 9762169at2; -. 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; cd00161; RICIN; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.80.10.50; -; 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; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. 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 Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAJ58949.1}; 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:CAJ58949.1}; KW Transferase {ECO:0000313|EMBL:CAJ58949.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 343..362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 9..266 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 273..300 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 380..474 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 611 AA; 63097 MW; B3083AD500CAEF93 CRC64; MARRLGSSYI LETVIGRGAM GEVWRGRDED GAPLAFKLLL PELMVDPQIV ARFMRERSVL LRVDSPFVVR VRDLVAERGD LAIVMDFIEG SDLRRELIRR RTVPPSEAVA TIVDILTGLD AAHELGIIHR DLKPENVLLD RHDGGYRPKI SDFGIAGLTD ASTRLTIGPG LLGTPLYMAP EMIEEGVAGP PADIYAAGLM LYELLCGVTP FSGRAPLALL RAHVDLLPGR PPNLSDELWS VLAAMLAKDP AERTGADQLR ALLPDLHGLP ASPPLATPPL ATLTPGSLPP ATLPPIAVPP DAVPSDASLL DAVPPDAAVA IGPDPDRPGH SSAEPGGRGR RRLLVVALGI VVVIVATAAA LVSTTGSSSD PSRRLLIQAG TRDQQARAGQ PAATAGPSPG ASARADGAGS PAPTSMPASA STPEPGSGLA PEPGSGLAPG SAPQPAPAPA SAVRVAHPTA PPPQRPAGPA VAAPPAVAAP AQGVLGRTFT DVATHSCLDS NAQGQVYTLG CNQGNYQHWV YAAGNDGVRL RNAQTNNCVG SRANPAPDGT RYQGTVYAIG CDGGAAQLWT TSSDGAGMTF RNAATGECLD SNADGRVYTQ GCNHGDYQRW G //