ID PKN1_COREF Reviewed; 660 AA. AC Q8FUI5; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Probable serine/threonine-protein kinase CE0033; DE EC=2.7.11.1; GN OrderedLocusNames=CE0033; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(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 -!- 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; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; BA000035; BAC16843.1; -; Genomic_DNA. DR RefSeq; WP_006768658.1; NZ_GG700684.1. DR AlphaFoldDB; Q8FUI5; -. DR SMR; Q8FUI5; -. DR STRING; 196164.gene:10740422; -. DR KEGG; cef:CE0033; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd06577; PASTA_pknB; 4. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1. DR Pfam; PF03793; PASTA; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 4. 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; Kinase; Nucleotide-binding; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..660 FT /note="Probable serine/threonine-protein kinase CE0033" FT /id="PRO_0000171196" FT DOMAIN 9..278 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 377..443 FT /note="PASTA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 444..512 FT /note="PASTA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 513..577 FT /note="PASTA 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT REGION 288..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..319 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 15..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 660 AA; 69647 MW; D33D797EB02D44B1 CRC64; MTFVIADRYE LGASIGSGGM SEVFAATDLL IGREVAVKML RTDLAKDVNF RERFRREAQN AGKLSHPSIV AVFDTGEVDR DGISVPYIVM ERVHGRDLRD IVREDGPYSP SQAATIMIPV CHALQSSHEA GIIHRDVKPA NIMINNTGGV KVMDFGIARA LDDSTSAMTQ TAAVIGTAQY LSPEQARGKP ADARSDVYAA GCVLYELVTG RPPFEGESPF AVAYQHVQEE PTPPSEYISD LSPTAALNVD AVVLTAMAKH PADRYQTAAE MAADLELLSR NAVSRAARAH VEKPDEPETV VVPQRLSTPP PPPTPAMPAA TVAAPAAAPT AVGSRPAAAR QPKRGSRALT VLAIVLTLGV IGVGGAFTYD FLSNSSSAST QQIPNIVGLP ENEAVLELER LGFTVVLTTE PSPDVAEGLV IRTSPNVGSE IREGATVTLT ISSGREVVTI PDVTGLTLAE ATREIEGAGL VLDQSIREEN SDDYPAGTVI QQNPRAGGET SVGASITLTV STGPSLVRVP VITGMQWSQA ESNITSLGLV PDIYYVDSLL PEGQVISASG QGTELPRGST VTVEISNGML IEAPDLARLD VDNALKALRD AGWTAPDTSL IEGAPIPTGA LVDQGRIGFQ DPSPGQPLRK DAVVNIRLYR FDLTALVPEP //