ID Q81ZX3_STRAW Unreviewed; 583 AA. AC Q81ZX3; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 134. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAC72534.1}; GN Name=pkn17 {ECO:0000313|EMBL:BAC72534.1}; GN ORFNames=SAVERM_4822 {ECO:0000313|EMBL:BAC72534.1}; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC72534.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC72534.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces avermitilis: RT deducing the ability of producing secondary metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] {ECO:0000313|EMBL:BAC72534.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). 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; BA000030; BAC72534.1; -; Genomic_DNA. DR RefSeq; WP_010986245.1; NC_003155.5. DR AlphaFoldDB; Q81ZX3; -. DR KEGG; sma:SAVERM_4822; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_1_11; -. DR Proteomes; UP000000428; 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; 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:BAC72534.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000428}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC72534.1}; KW Transferase {ECO:0000313|EMBL:BAC72534.1}. FT DOMAIN 15..272 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 305..404 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 436..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 558..583 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..369 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 563..583 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 583 AA; 58766 MW; 94FD7991762ADABF CRC64; MQPLEVGEPT VVGPYRLLGR LGSGGMGRVY LGRSTGGRTV AVKIVHPHFA LDEEFRARFR REVEAARRVG GAWTAPVLDA DPEASVPWVA TGYAAGPSLA AAVTDGGPLP THSVRALGAG LAEALSAVHG LGLVHRDVKP SNVLLTLDGP LLIDFGIARA TDGTASLTST GVSVGSPGYM SPEQILGKGI AGAADVFSLG AVLAYAGTGA PPFPGDSSAS LLYKVVHEEP ELGSLEGELR ELVAHCLAKD PDGRPGPAEV AERLAPQGAA RLVTGGWLPG PLVEQVSRSA VQLLNLDVAG AAEAVPSGPV EFSTPSVRPP TGVFGPPPDL ATPAYMPAPR PAEAQPRPEP QPQPQPQPQS QPPAQPQDAV PGVPLAVAPE SGPPGRVSVS VAATSAPGTG GRGRRVSCTV ALAVAGALAT VTVGSAFLFG LLEGGDSSGG DSSGSADSPP AATASASRSD PGDGADGAVP KSYLGTWEGD ALALGGTLPA GTFRVTIGEA AVGKEIGTFR STDQLGGTCD DVLLLKKATA QQLVATSVAK DTNPSTCTTG RHEVRLTPVG DDLSYETDNQ AAGNPTSRMS KVK //