ID A1SM32_NOCSJ Unreviewed; 545 AA. AC A1SM32; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 92. DE SubName: Full=Protein kinase {ECO:0000313|EMBL:ABL82867.1}; GN OrderedLocusNames=Noca_3365 {ECO:0000313|EMBL:ABL82867.1}; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL82867.1, ECO:0000313|Proteomes:UP000000640}; RN [1] {ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; 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., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABL82867.1, ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; RX PubMed=21551312; DOI=10.1128/JB.05109-11; RA Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A., RA Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S., RA Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A., RA Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R., RA Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.; RT "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete RT Nocardioides sp. strain JS614."; RL J. Bacteriol. 193:3399-3400(2011). 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}. 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; CP000509; ABL82867.1; -; Genomic_DNA. DR RefSeq; WP_011756801.1; NC_008699.1. DR AlphaFoldDB; A1SM32; -. DR STRING; 196162.Noca_3365; -. DR KEGG; nca:Noca_3365; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_6_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000000640; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. 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; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABL82867.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000640}; KW Transferase {ECO:0000313|EMBL:ABL82867.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 343..374 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 419..438 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 443..460 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 480..499 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 17..269 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 45 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 545 AA; 57968 MW; 11D65AA0ED719680 CRC64; MTTTPQPSPP RRSVGGYTLL ARLGEGGMGV VHLARREAGE RVALKVLRPH IVGDEEARRR LAREVGSLSR VRSQWVAEIV DADPWAEVPY VATRYVPGLS LHDHVVEEGA ITGADLLWLA SCLAEGIASV HAVGVLHRDV KPSNVLMEGR TPILIDFGLA RVADDPKLTH TGWLLGTPGY LAPEILYGED ATVASDVHSW AATVAYAGTG HPPFGRGPSM AIMDRVRRGQ FDLDGLPHDL HQVVAAALDP DPRERPSLEQ ILAWLRPLTT RPGEPRTLPP TAPPHDPYTV PLALAAQAAA DDETDVWPGH NSAEPYTLAL TSYDAPVPAA PAVSLGERLR RGLLLVGLAL TAGTGSAAFP WITLALLLVT VWLLRSGSLA GSARDQRREY RGRKWYDGVQ LLVATPWHLV QSLPGTLLLA LWSVGLAVAA ALVCYAVATG LALALFVCGT ALTVSLWLGP GGSRVRGPVS RVVNPLAADP RRWVIALLLV LAVAAGLGFR ADLTGTTWTP ADGRPHAEKS SPGAGERGTM VAMQHLAISS EIIIS //