ID Q0RFM1_FRAAA Unreviewed; 755 AA. AC Q0RFM1; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 02-SEP-2026, entry version 92. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN OrderedLocusNames=FRAAL5081 {ECO:0000313|EMBL:CAJ63721.1}; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales; OC Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63721.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ63721.1, ECO:0000313|Proteomes:UP000000657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45986 / CECT 9034 / ACN14a RC {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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; CAJ63721.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RFM1; -. DR STRING; 326424.FRAAL5081; -. DR KEGG; fal:FRAAL5081; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_11; -. DR Proteomes; UP000000657; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd06577; PASTA_pknB; 4. DR CDD; cd14014; STKc_PknB_like; 1. DR FunFam; 1.10.510.10:FF:000021; Serine/threonine protein kinase; 1. DR FunFam; 3.30.200.20:FF:000035; Serine/threonine protein kinase Stk1; 1. DR Gene3D; 3.30.10.20; -; 4. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. 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; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF34; SERINE_THREONINE-PROTEIN KINASE YBDM-RELATED; 1. DR Pfam; PF03793; PASTA; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 4. 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}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}. FT DOMAIN 34..302 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 463..530 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 531..598 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 599..669 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 688..751 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 414..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 670..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 161 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" SQ SEQUENCE 755 AA; 78238 MW; 0CCF09B17E8C166D CRC64; MAPVAAWFGN DRKLSPVDAT VADPVIGRLL DGRYTAQERL AVGGMATVYV AHDNRLDRLV ALKVMHPNLN HDPEFVGRFH REAKAVARLN TPRVVSVLDQ GSDHTSAGLI NYLVMELVRG RSLRQHLGAR GRLSVAEAVE IIEPVMEALA AAHDAGIIHR DIKPENILLG DDGQVKVADF GLARPLGQPT QALTDGVVMG TVGYLAPEQV TLGTADTRSD VYAAGVVLFE SLTGHLPHSG ATPMSMAYQS VHGDVPAPST IVEGVPAELD GLVLRATARD PARRPADGAA LLDELHRIGP YLPAPDSYQT GFTGEVERIG LMAPPPEDPG PDHTRPFQPT DYDNDYNTGY GADHDTGYDG PHGAAGFTGA EAGRPRAGIA EHDSAAGAPY AGGVASQPGT GALYRSAAAP TPTSTSYLGA GHGRRRAAGP GSGAGPRRYL PLAVGGAAIL VLLIGFLAVR MLSSDKVEVP LLTSVSKSDA ETMLRDAGLK ATYLDPIASP KVAAGHVAQQ DPRDGTKVDK GAVITLRLSS GPATVPVPDL ANLTRDQAAA RLNEVNLAVG GQINQASDTV PAGHVIGTNP AVNTVLKPRD GVTLIMSSGP DTRQMPADVI GKPYDAAKAE IDALGVAGVT VQRDLAVTED TPAGNVVGAA PGVGQPIAPN TVVTLTVATA PDDGTDTSGT SDGGDGSGVQ VVVPKVVGKT YREAEGILAQ RGLKIDRFAP FGKPNDRVTA QSAQPNSKIE KGSTVHVNTV WQLGN //