ID A0LTE4_ACIC1 Unreviewed; 543 AA. AC A0LTE4; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 77. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABK52704.1}; GN OrderedLocusNames=Acel_0931 {ECO:0000313|EMBL:ABK52704.1}; OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B). OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae; OC Acidothermus. OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52704.1, ECO:0000313|Proteomes:UP000008221}; RN [1] {ECO:0000313|EMBL:ABK52704.1, ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / DSM 8971 / 11B RC {ECO:0000313|Proteomes:UP000008221}; RX PubMed=19270083; DOI=10.1101/gr.084848.108; RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V., RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C., RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.; RT "Complete genome of the cellulolytic thermophile Acidothermus RT cellulolyticus 11B provides insights into its ecophysiological and RT evolutionary adaptations."; RL Genome Res. 19:1033-1043(2009). 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; CP000481; ABK52704.1; -; Genomic_DNA. DR RefSeq; WP_011719767.1; NC_008578.1. DR AlphaFoldDB; A0LTE4; -. DR STRING; 351607.Acel_0931; -. DR KEGG; ace:Acel_0931; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_035480_0_0_11; -. DR InParanoid; A0LTE4; -. DR OrthoDB; 3778994at2; -. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR032710; NTF2-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR PANTHER; PTHR43671:SF116; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF54427; NTF2-like; 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:ABK52704.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008221}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK52704.1}; KW Transferase {ECO:0000313|EMBL:ABK52704.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 333..353 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 25..288 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 279..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 360..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 543 AA; 56787 MW; DA113E527E7A642B CRC64; MRLGESLNDE TSHDVGALPP RLAGYDVSEL VAIGRYAAVW RARTAVGDRS VALKRPHATR EAAARVVHEA AILRAARHDH VVAFLGLERE PWRQPAPGLP CQCPVLVTEY AEGGTLAELL ANRIRLSPAE VVTLGVPIAR ALDLLRRRGI RHGDLRPANI AFTADGKPLL IDFGHARWCD APQRRGRRGE RRPGVAGPDP DDVRAFLDLL RLALIGAPPP EPSPPLGVLA GDIPEPLSRL LELAAATDPT TLGLETFARE LLAACTPAPI TLVSRTAASR SVSPTPEEAG EAASAGASVA PSPGRRSHWA VKLAGAHRRR RSSPVRLSST RTGVVVGAIA VLAVAALAAL ALVRTGHATA RPAQLEPADA VAATPQESGH DPARGSPEGP SVSAPSDGIP ARQPADARGT PDWPGVVAEL YARRAHALIN RDPALLATVY TPTSPLAAAD GETVAGLRAV GARVEGFAPR VLSVDVIQAD RTTAVLRVTD QLPPYGVATS GGRQANPGRG PVTRLITLRY VDGEWLIDAI DLAAPVNGPT GSS //