ID Q10YD2_TRIEI Unreviewed; 664 AA. AC Q10YD2; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 116. DE SubName: Full=Serine/threonine protein kinase with WD40 repeats {ECO:0000313|EMBL:ABG52742.1}; GN OrderedLocusNames=Tery_3681 {ECO:0000313|EMBL:ABG52742.1}; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Oscillatoriales; Microcoleaceae; Trichodesmium. OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG52742.1}; RN [1] {ECO:0000313|EMBL:ABG52742.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG52742.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Richardson P.; RT "Complete sequence of Trichodesmium erythraeum IMS101."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000393; ABG52742.1; -; Genomic_DNA. DR AlphaFoldDB; Q10YD2; -. DR STRING; 203124.Tery_3681; -. DR KEGG; ter:Tery_3681; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2319; Bacteria. DR HOGENOM; CLU_000288_135_4_3; -. DR OrthoDB; 500858at2; -. 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 CDD; cd00200; WD40; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. 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; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50978; WD40 repeat-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; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 7. DR PROSITE; PS50294; WD_REPEATS_REGION; 6. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABG52742.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABG52742.1}; KW Transferase {ECO:0000313|EMBL:ABG52742.1}; KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE- KW ProRule:PRU00221}. FT DOMAIN 34..301 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 374..415 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 416..457 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 458..499 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 500..541 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 542..583 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 588..629 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 630..664 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 302..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 65 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 664 AA; 73892 MW; 2817F1DDC5F5C30F CRC64; MSYCLNPQCQ NPQNPEGTLY CIACGSKLLL RERYRPIKPI GRGGFGRTFF AVDEDKPSHP PCVIKQFLPQ NTGDPKKAAE LFQQEAVRLD ELGKHPQIPE LLAHFEQDNY QYLVQEFIDG SNLAQESIKN GPFDSNQIQQ MLNELLPVLK FIHEQKVIHR DLKPENIICR SSTPETIGWM TNTNKLVLVD FGAAKVITGT SLMQPGTIIG SPEYVAPEQL RGHAIFASDI YSLGVTCIYL LTQISPFDLF DVMADKWVWR DYLNQPFNSK LGKVIDKMLM TNPQIRYQSA LEVMKELNPT QAFPTAPNTF PPTASTTKRS TSSPIPNRPT MATYTSPKQP TKQSTNSITA PPYVIQPTVL PQPQQSTWKC VLTLTGHFDS VNSVAFSPDN QILASGSRDK TIEIWDMTKG KRWFTLTGHG NSVSSVAFSP DNQMLASGSR DKTIEIWDMK KGKRWFTLLG HSDWVDTVAF SPDNQMLASG GRDRAIEIWN LQKARRWFTL AGHQDRVYTV AFNKDGGILA SGGRDQTIKI WDLQKAKELF SIQGHSDWVR SLSFSPDGGV LGSGSRDGTV KLWQVYGGEL ISTPIQHLKY GVSDVLSVGF SPNGKIVAAG YRNGVINLWD AVTGELLETL NGHSSDVFSV VFSQDGRSLA SGSNDKTIKI WQVP //