ID Q01QY7_SOLUE Unreviewed; 937 AA. AC Q01QY7; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 97. 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=Acid_7020 {ECO:0000313|EMBL:ABJ87933.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae; OC Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ87933.1}; RN [1] {ECO:0000313|EMBL:ABJ87933.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ87933.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Janssen P.H., Kuske C.R., Richardson P.; RT "Complete sequence of Solibacter usitatus Ellin6076."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; CP000473; ABJ87933.1; -; Genomic_DNA. DR AlphaFoldDB; Q01QY7; -. DR STRING; 234267.Acid_7020; -. DR KEGG; sus:Acid_7020; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0823; Bacteria. DR HOGENOM; CLU_012906_0_0_0; -. DR InParanoid; Q01QY7; -. DR OrthoDB; 114067at2; -. 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; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR011659; PD40. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1. DR Pfam; PF07676; PD40; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00320; WD40; 3. DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1. DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ87933.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ87933.1}; KW Transferase {ECO:0000313|EMBL:ABJ87933.1}. FT DOMAIN 79..350 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 937 AA; 101290 MW; CE17B2806F33CA9A CRC64; MGTPDEADLK AQLWRRAYEI FDDGLETPSE QRHDFARARA SGDPELLEIV FELLQNAREE DLDGVEEQEP RIGSKLGRYQ ITAKLGRGGM GQVYAAHDSE LGRLVALKLL SGQTGSPGKM GSAERLIREA KAASALNHPN IVTVYDVVRH GSEVALAMEL VEGQSMREVC GQPQPVGQVI HWARQIVQAL AATHARGIVH RDIKPENVML RPDGYVKVLD FGLARRTRLL EGAPSASASL FGFLGGTLSY MSPEQARGEN PTQASDIFSL GSMLYELLCG VHPFQSASPI DTAYAIAHHE PKRAGSVRPE ISAALSSLVA AMMAKDAADR PAAVELEQLL KLSGTPEPFT RRRRAPAMAA LSIALLLVAA GAVFLRQPLE TPKPLVLDPL TRLLDKNVTA AALSPDGTQL VYALFGGPLY LRRMSDGGTR ILHSPAGLRA SRLAWFADGK QLLISGAGDD RKLALWVLPL DSLERDAVLV PHQGRDAAPS PDGSRIALCS SDGSAIRIVD RDGSHPRVIR SAEPGANFHS LVWSPDSKRI SYMILTQVAR PPAKYSFVFE TVDAESGLLI ARIDDLPLFS ATALPDGRII GLPWAYPATS HGGELIEIRT NPSTGAVIGQ SRTPMPYSKD GMFSSLTVSN NGGTMALISA SEFVNIYAAE FAAAPVPALS NVRRLTFGLT QDYPQSWTPD SKAILFESNR NGRFELFRYE LSSGRETMFY RGREDAVQPR VTPDGRWILF RQGASRFAAQ LMRLPVDGSA QAAPVPMAGE TGAEQGCGAA PASRCVVRSV EADQFVVREL DPVQGKGRVL ARTPYGPYLI FDWSLSPDGS VIASPNHDSQ SALIRLTPLD ARIDERFIKL EGFRNLSSVS WSADGKGLFV TANAGSGGIM IYSDLEGHAS QLLESSKVTF VVPSPDGQRI AYPEQVTSST VQLLRRP //