ID PKN2_CLOPE Reviewed; 685 AA. AC Q8XJL8; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Probable serine/threonine-protein kinase CPE1738; DE EC=2.7.11.1; GN OrderedLocusNames=CPE1738; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh- RT eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). 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; BA000016; BAB81444.1; -; Genomic_DNA. DR RefSeq; WP_004458146.1; NC_003366.1. DR AlphaFoldDB; Q8XJL8; -. DR SMR; Q8XJL8; -. DR STRING; 195102.gene:10491002; -. DR KEGG; cpe:CPE1738; -. DR HOGENOM; CLU_000288_135_2_9; -. DR Proteomes; UP000000818; 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; 3. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 3. 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; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. 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..685 FT /note="Probable serine/threonine-protein kinase CPE1738" FT /id="PRO_0000171195" FT DOMAIN 10..275 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 376..440 FT /note="PASTA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 441..508 FT /note="PASTA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 513..581 FT /note="PASTA 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 589..648 FT /note="PASTA 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT REGION 277..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 480..500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 623..685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..329 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..500 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 623..639 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..685 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 143 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 16..24 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 685 AA; 74576 MW; 75A396084485EB24 CRC64; MIGKILGNRY ELLQCVGEGG MSFVYKARCR KLNRFVAVKI LKDEFKNNEE IVRRFKKEAT AIANLSNPNV VNVLDVGTQD DINYIVMEYV EGKTLKDIIK EKGALPYEVA ISIGIKVAKA LECAHKSGII HRDVKPQNIL VTEEGVVKVT DFGIAKSMDS STIAHTNSVM GSAHYFSPEQ AKGTYTDYRT DLYSLGIVLY EMVTGVVPFN GDSPVTVAVK HIQEKAIPPK NINQNIPNSL NDLIMKAMEK DPVNRYQTAK EIIGDLEKIK KDPNVTISSK SAEDEDQFTR VMSPVVVPNT ETNNSEPDED DEDDDEYYED DEDEDEEENN IQTKPQKAIN KNKKKSPILI IIATILVVAL GITLGFLGMK KFMEGGKDVK IPNVVGEKVE DAKSKLEGLG LKVLEVTEES DQEKGIVLKV DPNVDSTVKT GSEVKLTVSG GEGQIKVPNF AEMNLDSVKR TLKSLGLELG SVDEEYSDSV PRGEVISQSP NANESVDKGS KVNVTISKGK EIKSETINIP DVSGKSVEEA KSILANAGVG VNPVKGEAAK SEGEAGKVYS QSQSGSLTIK QGEKVTITIN YYGDYVKPEK PKHNAGELVG MTGAQAKAWA SKNKINVSGI TSDTAKVKSV SNSGEVEEGG SVSVTMEEEK KPEQPTQPNQ PTQPTQPNQQ AQPEQPKQPE QSGNN //