ID Q0RG05_FRAAA Unreviewed; 933 AA. AC Q0RG05; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 119. DE SubName: Full=Putative serine/threonine-protein kinase {ECO:0000313|EMBL:CAJ63584.1}; DE EC=2.7.11.1 {ECO:0000313|EMBL:CAJ63584.1}; GN OrderedLocusNames=FRAAL4943 {ECO:0000313|EMBL:CAJ63584.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63584.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ63584.1, 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 -!- 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; CAJ63584.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RG05; -. DR STRING; 326424.FRAAL4943; -. DR KEGG; fal:FRAAL4943; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2319; Bacteria. DR HOGENOM; CLU_000288_135_4_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: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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008266; Tyr_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; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00400; WD40; 3. DR SMART; SM00320; WD40; 6. 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; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000313|EMBL:CAJ63584.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000313|EMBL:CAJ63584.1}; 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 509..531 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 45..296 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 687..728 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 732..773 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 777..818 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 298..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..452 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..476 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 933 AA; 93879 MW; 178429385E5E172C CRC64; MRGGACGAEA APREWGTVTG TTPPPLSGNT ARPLQPEDPR RLGTYQVVGR LGQGGMGTVF LGRAPDGTAV AIKVIRPELA QRPEFRARFA REAESARRVR RFTTAAVLDA DPHGPQPYLV TEFVEGPTLS RHVSVRGPMR PADLEQLAVS VTTALSAIHA AGIVHRDLTP GNVLLSPVGP KVIDFGLARE FNADTELSRN VRQAIGTPGY MSPEQILDAP ITSAVDIFSW GAVMVFAATG QPPFGTGRME AILYRIINEP PRLDGVSGEL RGLIEVAMAK EAGARPSAEE LRTALIGGGA LPARPTPVTT PDEPADAAAA QPRRWGRRGR DTATSTPPVQ PPGTAGAGSV TGSEGAAGRS APGRFTGSAG ASGSGRSVAP HAAPGGAATD APAGSFGGRP ATAVPPPTAG GGPPAGAMPA TQMSPAPLAS PPPVPSRTPP PGNPPPGGLP PGAVSPGAVS GSVPSAAPSA SSPGSVPPRA QGPGDAYAPP GGAAGDAQPG PRRRRPRTLV LAAAFVVLLA AAVAIPVLVL GGGDGPGAPN PAERAAASAR LATDAAARRA QDPQLAARLS LAAYAVAPTA AARDSLIASF GQSTAVRVPA GAAAYSDLAL SADGTALAGT DDAGRLHLWR LDGEGRPTVA AQGSADDHAS GVVFDGGGRT LATGGATDAG RLWDVSDPAR PRPLGALGTQ STPVHRLALS TRAHLLATAG VDWSVGLWDV TDPSRPTSLQ LLIGRSGPVT GVALRPDGAV LAIAGVGGTV QLWNVRDPRS PTQMGSVPGH TGAVNTVAFS PDGTLLATGG DDRNLQVSDV TDPNRPRVVH RLPGHAAPVT TVAFATDDQL LSADSAGSVA YSNLAATGPA LIPVGTLDSP VRAMSTSTTG TVALTTDRGT ILLGTVDPQR LRQRACAKPG AAPSRTEWSR LVPGIPWSDA CAS //