ID A0K290_ARTS2 Unreviewed; 295 AA. AC A0K290; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 102. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABK05410.1}; GN OrderedLocusNames=Arth_4035 {ECO:0000313|EMBL:ABK05410.1}; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Arthrobacter. OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK05410.1, ECO:0000313|Proteomes:UP000000754}; RN [1] {ECO:0000313|Proteomes:UP000000754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754}; RX PubMed=24501649; DOI=10.4056/sigs.4438185; RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T., RA Han C., Beasley F., Chen W., Konopka A., Xie G.; RT "Complete genome sequence of Arthrobacter sp. strain FB24."; RL Stand. Genomic Sci. 9:106-116(2013). 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; CP000454; ABK05410.1; -; Genomic_DNA. DR RefSeq; WP_011693858.1; NC_008541.1. DR AlphaFoldDB; A0K290; -. DR STRING; 290399.Arth_4035; -. DR KEGG; art:Arth_4035; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR Proteomes; UP000000754; 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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1. 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. 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:ABK05410.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000754}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK05410.1}; KW Transferase {ECO:0000313|EMBL:ABK05410.1}. FT DOMAIN 21..284 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 295 AA; 31484 MW; F19C25C204810FF5 CRC64; MTSDCGGQPP EIWDAGSDTR YLLHERLGVG ATAQVFRGTG HRDGRPVAVK VAALADKRNG ERIAAEAVLM EGLRHPALVK FVDKGTGAAD SRWAGHPFLV QELVYGSSLA ETIRWGPVPG SEVAPWAVGL LSGLRHLHAR GIVHRDIKPA NLLLSRLRKC PVRIIDFGIA APAGTEPEPG TSSGTVQYMS PEQANGETVR PADDIYALGL VLLECLTGVK AFPGTAVESL VARTLRSPGI PQHLGSQWAS LLGSMTARHA AERPTALEAT AEAAMLLQRP HPLRRRVEAR SGSYC //