ID Q47N62_THEFY Unreviewed; 617 AA. AC Q47N62; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 114. DE SubName: Full=Tyrosine protein kinase:Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ56107.1}; GN OrderedLocusNames=Tfu_2074 {ECO:0000313|EMBL:AAZ56107.1}; OS Thermobifida fusca (strain YX). OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56107.1}; RN [1] {ECO:0000313|EMBL:AAZ56107.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YX {ECO:0000313|EMBL:AAZ56107.1}; 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 --------------------------------------------------------------------------- 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; AAZ56107.1; -; Genomic_DNA. DR AlphaFoldDB; Q47N62; -. DR STRING; 269800.Tfu_2074; -. DR KEGG; tfu:Tfu_2074; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_513711_0_0_11; -. DR OrthoDB; 3415202at2; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 PANTHER; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:AAZ56107.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ56107.1}; KW Transferase {ECO:0000313|EMBL:AAZ56107.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 420..442 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 31..277 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 343..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 445..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..414 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 617 AA; 63789 MW; E81E34BA5CC7A594 CRC64; MSRRSERTIS VLVPPDLAPT APEDPRTIGP YVLVGRLGAT ETGSVYAAVH PDVEPEALLA VKVIPSSRVA DEAARTRLEQ RLRTLGAVDG RCYVPPVAFD VHGTPPWLAT RYSPGTPLKQ YIDQRGPLRL GRLTALAAGL GEALSALHSL DVVHGDLKPS SVLLSSAGPR LLDCALSGEA PAPAGSTPWL SPERLRGEAP TPASDVFSWG AVLAFAATGK PPFGTGTPEE VAERIASGSP DLSDAAEEIR SLLESALAAD PAERPNIREL VRSSISLWES SLGTVGSEAG PGSGVTRVLT REWQGIVEPA LLPRVVHLDD RARGKKSGLR SLTMPVPLLS RSTAQPASSA AAADAPDSTG PTSSGAAATA VTAQEDTEAN TDTPAKAASA PSSSSSAPAA PPASSPSTGP SGSKGPNKRF LALVGGGAAA ALLLLGGGVW AVSALRGDDP EPQDVTAQPD SAPEEAPQEE PPPAWDTGTL VVRLDSSSDV HLLAGPWPYT PVKPASGDDA FAGLNGREVT PEEWSEAWAP VPGVEEPLEA LIASDAEVMC AHFCLNPDQV YVDEEGRGTY KVTGRDLGNY LSWGDAVIAE VTFGEPDPET GLPVITKVTE LYPLPTA //