ID Q81ZZ0_STRAW Unreviewed; 568 AA. AC Q81ZZ0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 136. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAC68685.1}; GN Name=pkn2 {ECO:0000313|EMBL:BAC68685.1}; GN ORFNames=SAVERM_975 {ECO:0000313|EMBL:BAC68685.1}; 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:BAC68685.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC68685.1, 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:BAC68685.1, 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; BAC68685.1; -; Genomic_DNA. DR RefSeq; WP_010982413.1; NZ_JZJK01000073.1. DR AlphaFoldDB; Q81ZZ0; -. DR KEGG; sma:SAVERM_975; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR OrthoDB; 9762169at2; -. 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; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1. DR PANTHER; PTHR45832:SF25; SERINE_THREONINE-PROTEIN KINASE SAMKA-RELATED; 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:BAC68685.1}; 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:BAC68685.1}; KW Transferase {ECO:0000313|EMBL:BAC68685.1}. FT DOMAIN 15..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 281..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 382..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..301 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 313..330 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..421 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 568 AA; 60378 MW; 8EE92FFDF2E880DB CRC64; MGEGETGRRV VDNRFELEAR LGGGGMGTVW RARDLLLHRS VAVKEVRPPD VDFAEYDPDG AHLLRERVLR EARALARVEH PNVVTIHHIV DGGEGTYPWI VMELVGGGSL ADRLARGPMT PAEAAHIGRG VLAALRAAHA AGVQHRDVKP ANVLLRPDGS PVLTDFGIAA IRESTTLTAT GSIIGTPDYM APERVTGDRG GPGADLWSLA MMLYVAVEGH HPLRRGTTLA TLAAVLHDDV PHPVKAGPLT PVLTRVLVRD PAARPDAEAF DRMLAAVAEA GPGAEPTSYP LAPPVPAPPP ATTESGLVGA SRNPRDHLRR PAREPRDAVP DPRPPLGSDA DRLGTRTVTR RPGRARLIVV ASVAGASLVG GLVWRTLPGG QDGAAASPGA SRETEHAPAA PTTVTQKPTD QESDSETTDL LTPAGIRASI KAIEKETGRD SFGDFSVYPD HVSASVMVEG SRTRYDTYTY RVDRGVEKGI IKGTLAGGRQ PVSLKNFQWD MVPALLARAE RALKVEKPTA RYLLVRQPDN VFGTPAGMAV YLSNDYREGG YLEADTQGKV TKVMPAAG //