ID Q020M0_SOLUE Unreviewed; 841 AA. AC Q020M0; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 95. 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_3661 {ECO:0000313|EMBL:ABJ84633.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae; OC Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84633.1}; RN [1] {ECO:0000313|EMBL:ABJ84633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84633.1}; 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; ABJ84633.1; -; Genomic_DNA. DR AlphaFoldDB; Q020M0; -. DR STRING; 234267.Acid_3661; -. DR KEGG; sus:Acid_3661; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0823; Bacteria. DR HOGENOM; CLU_012906_0_0_0; -. DR InParanoid; Q020M0; -. 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 PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF07676; PD40; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2. 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:ABJ84633.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ84633.1}; KW Transferase {ECO:0000313|EMBL:ABJ84633.1}. FT DOMAIN 19..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 841 AA; 89955 MW; 41DB8F359E16A4A7 CRC64; MGTDTIEPLF TPGQKLGPYE LLTPIGEGGM GQVWKARDTR LGRTVAIKVS KTSFSERFER EARAVAALSH PNICTLYDVG PDYLVMEYIE GKPLKGPIPV ETALRHAIEI AKALDAAHRL GIVHRDLKPG NVLVTRTGIK LLDFGLAKVT TAAAAASEET VTRALTEEGT ILGTLQYMAP EQLEGKEADA RSDIFAFGCV LYEMLTGAPA FTGGSRASII AAIMDREPKA LPEAPASLES AIRQCMAKDP DERWQSARDL AGVLELAGVT PPAVTIVRAP KAALAVLAVV AALAIAAAIW FAQHKPQEQF WSGQSLGGPA QAFGPRVSPD GQTIAFQAMV DGQTQVAIMK PESGNWTVLT HQKNLGQIQD ITWSRDGSKL YFDRVTDTPR GVFSVPLLGG ESRRVLEYGS YPSVLADGSL VVGMINPQRI LQLHRYWPES GKLVPLPGVP DTASAAAGRA TPDGKSIVFY GNPLDAKGNQ GPRGIYSLDP DSGRLLNLAP GQRLDGALAL AATPDGKSVV YSTQGRDFSS VISVPRNGSG EMRQLFTMTN IPLFLDAAPD GSIYADQLSH DTMILRYPPS GGIPERLTQL HGGAAVSLVL PDGRPLVYSV SGFKRRFQIV QPDGTLAPLI ESSEECGMPA ALVGEDRVAV LTDRKPIQIA IVSIADGRIM QRVTGPKDRL TSLSSSLDGK TLYYSSAGFI WSIPIEGGEP RQLAAGDNVS ADANGRDLIV SLQDKDAIRL LRMPVSGGTP LRIPLSGELR IPGTLLRASI VGPGGLIAVT TASSDRWMYQ TGLLDPRTGA LRRIPLNFDG ETQWPGWTRD GKLVSIGTVI GMSVWRFHAE H //