ID Q1IP04_KORVE Unreviewed; 736 AA. AC Q1IP04; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=Acid345_2395 {ECO:0000313|EMBL:ABF41396.1}; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Koribacter. OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF41396.1, ECO:0000313|Proteomes:UP000002432}; RN [1] {ECO:0000313|EMBL:ABF41396.1, ECO:0000313|Proteomes:UP000002432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF41396.1, RC ECO:0000313|Proteomes:UP000002432}; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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; CP000360; ABF41396.1; -; Genomic_DNA. DR RefSeq; WP_011523197.1; NC_008009.1. DR AlphaFoldDB; Q1IP04; -. DR STRING; 204669.Acid345_2395; -. DR EnsemblBacteria; ABF41396; ABF41396; Acid345_2395. DR KEGG; aba:Acid345_2395; -. DR eggNOG; COG0457; Bacteria. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG5616; Bacteria. DR HOGENOM; CLU_013589_0_0_0; -. DR OrthoDB; 6111975at2; -. DR Proteomes; UP000002432; 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; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR Gene3D; 3.40.50.10070; TolB, N-terminal domain; 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 InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. 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; PF00069; Pkinase; 1. DR Pfam; PF14559; TPR_19; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00028; TPR; 5. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50005; TPR; 3. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABF41396.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002432}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF41396.1}; KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}; KW Transferase {ECO:0000313|EMBL:ABF41396.1}. FT DOMAIN 9..285 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 534..567 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REPEAT 568..601 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REPEAT 643..676 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 736 AA; 81849 MW; ECD714A9A1DFB0C1 CRC64; MLGETVAHYR VLEELGGGGM GVVYKAEDSK LGRLVALKFL PADVTPDRGT LERFQREARA SAALNHPNIC TIHEIGEHQG RPFIVMELME GATLKHLIAG RPMRMDRMLE LGIQISDALD AAHAKGITHR DIKPANIFVT NHGQAKILDF GLAKLDGRGI RSRAAAGADL GVTISEDDLT SPGATLGTVA YMSPEQARGE TLDARTDLFS FGAVIYEMTS GNIPFSGNTT AVIFNNILNI SPKPLPQSIP DVPLELDRIV SKALEKDREL RYQTAAELRG DLRRLKRDTE SKGASASRVA AEPKAVSEQA AKSLAVLYFE NPGGTKDDEY FRDGITEDII TELSRIKDLW VLTRSAVMAY RDKPAASVEV GKQLNAAHVL EGSLRRSGAQ LRITARLVET ATARSVWAER YDRKLEDVFA IQDEIAQSIA KALKLMLTEQ EKRAIEKAPT ADVQAYDYYL RGRQFYYQFR RKSFDYARQM FARAIVIDPT YARAYAGVSD CCSHLYMYWG GSADDLKEAE AASRKAVELD PELAEGHVSR GLALQMVKKY EEAEAEFGKA TDLNPKLFEA YYFFARLCFQ RGNLEKAADL FERARLANPE DYQTPILLAQ TLESLERHLE AKAARARAMK LFERHVELHP EDARALYLGA SGLIDAKQMD RALDWTNRAL SIDPDDPAVL YNVACSYAKL AMSEKAMDCI EKALALGEYY KAWAEHDSDL DSLRSSPRFQ AMLKAI //