ID Q1J213_DEIGD Unreviewed; 362 AA. AC Q1J213; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABF44471.1}; GN OrderedLocusNames=Dgeo_0168 {ECO:0000313|EMBL:ABF44471.1}; OS Deinococcus geothermalis (strain DSM 11300 / AG-3a). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF44471.1, ECO:0000313|Proteomes:UP000002431}; RN [1] {ECO:0000313|Proteomes:UP000002431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431}; 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 Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.; RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000359; ABF44471.1; -; Genomic_DNA. DR AlphaFoldDB; Q1J213; -. DR STRING; 319795.Dgeo_0168; -. DR KEGG; dge:Dgeo_0168; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_0; -. DR Proteomes; UP000002431; Chromosome. 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABF44471.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002431}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF44471.1}; KW Transferase {ECO:0000313|EMBL:ABF44471.1}. FT DOMAIN 47..298 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 18..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 314..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..351 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 75 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 362 AA; 39762 MW; 407099138078F32B CRC64; MGEGRQSYVT IGLLSSNQPS ASGSFSTLRT PRLPLPPMTP ERTIPGYKLL YLLGRGHTAL VHLAQDAQGR QVALKIPLQD TLRVQEAAER FGNEVRLTLQ FRHPHVVQAY AGTPFGTQAF LALRHYPEGT LYDVLQRRGG QKLPLDEALR ILADVASGLT YLHALGAVHQ DVKTQNVYMD AGRAALGDLG STYFTAQGGQ SSGSPFYMAP EIYRGESSSP ASDVYSLGIL TYELLSGQRP YQGDTYEELM GAHLTRFAPP LVHLNPQVPR SLGRLAEQAL AKRPQDRPSA DTLRRAFLTG LGEPDEDEVL LEERSIPSQT PRPVGRHALA ARVPPPAEAA PNQPRLPEEP GPSRWNPFRR RK //