ID Q0RJ21_FRAAA Unreviewed; 803 AA. AC Q0RJ21; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=FRAAL3851 {ECO:0000313|EMBL:CAJ62494.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ62494.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ62494.1, 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; CAJ62494.1; -; Genomic_DNA. DR RefSeq; WP_011604986.1; NC_008278.1. DR AlphaFoldDB; Q0RJ21; -. DR STRING; 326424.FRAAL3851; -. DR KEGG; fal:FRAAL3851; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_1_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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd06577; PASTA_pknB; 3. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000313|EMBL:CAJ62494.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAJ62494.1}; KW Transferase {ECO:0000313|EMBL:CAJ62494.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 478..498 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 38..298 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 572..641 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 642..707 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 708..772 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 298..377 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 386..405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..440 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 452..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 507..575 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 739..803 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 312..336 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 784..803 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 803 AA; 79847 MW; 8C4CE271256C2C22 CRC64; MDARENVDEV TEPRETTTGL ATRPDPLRPG DPRELGEYRI LGRLGEGGMG TVFLGRGRDT GLVAVKVIRA DVARIPRYRD RFRREAAVAR RVARFCTAEV LDVVDPPDGQ PYLVTEFVDG PTLARAVATH GPLGSADLER VAVSVAAALT AIHGAGLVHR DLTPTNVLLS PLGARVIDFG LARVSDEAPS GPSGRVAGTP AFMSPEQARG ETVTSAADIF SWGGLVIFAG SGRKPFGDGP TSAQLRRVQH ADPTLGDLDP ALAAVVRAAM RREPAGRPTA EELLRRLVRP GDAAQTIVTS PLDILPPRTG LSISPPTSPP ASRTPPAGPP PSGSRPSGLA PSGSRPDLAP AVAGSGLAPA PAGSGPVPAG SKSGSAAAAR SGAGSAATAT GAGTGAGTGA GAGRRPGYAT GLAVARPEPA PGEGAGVAPA AGATEPDQTP AAVAVMPEPA TGPLDLMLAG PADPTDDRGP ADRRRVRLLT AVAGAVIAAT LLVIGLLVHA HGGPARATAS AAGQGAGPGV TATVHPVSPT TTRPATRPGG DGGARGDGGD AGTGAPTSTA DPAATTDPAD ASPATGRLLT VKNVVGQDAT VAETRLRELG FDTIERSYRA DDGARGTVVA IDPTPGTKAA RDTTVTLTVS TGPSTVTVPE VAHKSAAQAR AMLRAEGLVV VEQVITGRST ADAGQVDTAT PSPGSRVAAH STVTITVASD TVTVADLHGR TAADAERALT DLGLTVVEHP RTGGGQPGTV VGQTPAAGEV PRGSTVALDI ARPTATDSPS PPAAIGGSGP PTASPRPSPP ASP //