ID Q47TX0_THEFY Unreviewed; 742 AA. AC Q47TX0; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 142. DE SubName: Full=Tyrosine protein kinase:WD-40 repeat:Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ54094.1}; GN OrderedLocusNames=Tfu_0056 {ECO:0000313|EMBL:AAZ54094.1}; OS Thermobifida fusca (strain YX). OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54094.1}; RN [1] {ECO:0000313|EMBL:AAZ54094.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YX {ECO:0000313|EMBL:AAZ54094.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Lykidis A., Richardson P.; RT "Complete sequence of Thermobifida fusca YX."; RL Submitted (JUL-2005) 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; CP000088; AAZ54094.1; -; Genomic_DNA. DR AlphaFoldDB; Q47TX0; -. DR SMR; Q47TX0; -. DR STRING; 269800.Tfu_0056; -. DR KEGG; tfu:Tfu_0056; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2319; Bacteria. DR HOGENOM; CLU_000288_135_4_11; -. DR OrthoDB; 951193at2; -. 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; 3. 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:SF637; WD REPEAT DOMAIN 5; 1. DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. 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:AAZ54094.1}; 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:AAZ54094.1}; KW Transferase {ECO:0000313|EMBL:AAZ54094.1}; KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE- KW ProRule:PRU00221}. FT DOMAIN 16..266 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 464..496 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 497..538 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 539..580 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 581..622 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 623..663 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 664..705 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 706..742 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 266..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..316 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 323..372 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..392 FT /note="Pro 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 742 AA; 78950 MW; AC1734640DB4383D CRC64; MIEPLQPGDP GRIGPYRLVS RLGAGGMGQV FLARSPGGRP VVVKVILPEY ANDDEYRIRF AREVEAARRV GGFHTAQVID ADPTADPPWM ATAYIPGPSL RKAVTERGPL YGNNLRTLAA GLVEGLAAIH ACGLVHRDFK PSNIVLAADG PRVIDFGVAR PLDSSVMTQS GAVIGTLAYM SPEQTDGSQV GPASDVFSLG TVLAFAATGR SPFMADSIGE IIARISGPPP ELPELPDDLR ELVYACWEQN PDLRPTTAEL LAQLSTDHTG DDWPPPHLSD LIGSMLPLGA TTSPNPSLAI EPPPPSHGPP RPSEPLPDPG DDADEPSAEK PSRTLPEPEP PELEEKPIQV IHEPERPAPT PPRPREPARG AIKPKNPRPA APQPPWSPPR VQPPRWKQLI TKKPVAGILT AVATAGLVVS FLVWQWTLPE TPLRPDSSTA PSESADPHEL NEPRILTTDR EAVAVAFSPG GSLLAGGSGD KLIHVWDVAS GDELHTLEGH TDWVRAVAFS PDGALLASGS DDATVRLWDV AAAEERAVFE GHTHYVLDIA FSPDGSMVAS GSRDGTARLW NVATGTEHAV LKGHTDYVYA VAFSPDGSMV ASGSRDGTIR LWDVATGKER DVLQAPAENV VSLAFSPDGS MLVHGSDSTV HLWDVASGEA LHTFEGHTDW VRAVAFSPDG ALLASGSDDR TIRLWDVAAQ EEHTTLEGHT EPVHSVAFHP EGTTLASASE DGTIRIWPIA TE //