ID Q9KGI1_HALH5 Unreviewed; 327 AA. AC Q9KGI1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 132. DE SubName: Full=Serine/threonine-protein kinase {ECO:0000313|EMBL:BAB03799.1}; GN OrderedLocusNames=BH0080 {ECO:0000313|EMBL:BAB03799.1}; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558 {ECO:0000313|EMBL:BAB03799.1, ECO:0000313|Proteomes:UP000001258}; RN [1] {ECO:0000313|EMBL:BAB03799.1, ECO:0000313|Proteomes:UP000001258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 RC {ECO:0000313|Proteomes:UP000001258}; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). 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; BA000004; BAB03799.1; -; Genomic_DNA. DR PIR; H83659; H83659. DR RefSeq; WP_010896264.1; NC_002570.2. DR AlphaFoldDB; Q9KGI1; -. DR SMR; Q9KGI1; -. DR STRING; 272558.gene:10725903; -. DR KEGG; bha:BH0080; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_074074_0_0_9; -. DR OrthoDB; 583109at2; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 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|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000313|EMBL:BAB03799.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Reference proteome {ECO:0000313|Proteomes:UP000001258}; KW Transferase {ECO:0000313|EMBL:BAB03799.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303..324 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 29..273 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 269..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 269..286 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 327 AA; 37300 MW; E5718360D570B8F1 CRC64; MMKNNELKSL ASNLPSGTRI VGKWHKQRYR IIRKIGSGAT GTVYLAESIH GNVAVKVADS HYAITSEVNV LRHFQKVQGE RLGPSLLDVD DFVTPRGTIP FYAMEYVRGT NIVQFMAAKG EEWLGLLIVQ LLGDLDRLHQ AGWAFGDLKP DNLLVTGPPV RIRWLDVGGT TLLGRSIKEF TEFYDRGYWG LGTRVAEPSY DLFAVAMIML HCYDRKHFGK KEDKPLQQMK RKMDSIPQLK PFRPIMLRAL QSKYETAHQM REDMIQTLNH AGKETTSSVK TRPSRAAKRA SQNDRRNEKK SSYFVEIFLI ASFLLFLSIL YLFGQIM //