ID Q81ZX7_STRAW Unreviewed; 499 AA. AC Q81ZX7; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=pkn13 {ECO:0000313|EMBL:BAC72084.1}; GN ORFNames=SAVERM_4372 {ECO:0000313|EMBL:BAC72084.1}; 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:BAC72084.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC72084.1, 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:BAC72084.1, 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 --------------------------------------------------------------------------- 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; BAC72084.1; -; Genomic_DNA. DR AlphaFoldDB; Q81ZX7; -. DR KEGG; sma:SAVERM_4372; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR Proteomes; UP000000428; 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-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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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:BAC72084.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000428}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC72084.1}; KW Transferase {ECO:0000313|EMBL:BAC72084.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 362..381 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 19..285 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 322..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 382..499 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 382..398 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 422..477 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 499 AA; 52107 MW; 96CD021030E468C1 CRC64; MSDAPEMWGN GGLVGDGRYR LTGRLGRGGM AEVFAAEDVR LGRTVAVKLL RSDLAEDPVS KARFTREAQS VAGLNHHAVV AVYDSGEDVV GHSTVPYIVM ELVEGRTIRD LLLNAEAPGP EQALIIVSGV LEALAYSHQH GIVHRDIKPA NVIITHNGAV KVMDFGIARA LHGAQSTMTQ TGMVMGTPQY LSPEQALGKA VDHRSDLYAT GCLLYELLAL RPPFTGETPL SVVYQHVQDI PVPPSEVAEG APPELDGLVM RSLAKDPDDR FQTAEEMRGL VQYGLQMLYD QGGHTGTWNT GPVAVHEGRH TPAAGFANTT VLPHPSDSGT SQIPQPILPA YGGGDDGGFE GHGNRGTGRG KLWILAVLAV IAVAAGVALA LNNTGGSGTG TDTTKSPTAS HSSKDKESSK APSDEASDDS TDDNTGTGSD PDYPTPSYEQ SHSYSSQPSD EPTEPSNEPT DTTPTKPTPS TDPVTPSGDA SDPAETDGGG DGEGDTAGP //