ID Q47MC8_THEFY Unreviewed; 419 AA. AC Q47MC8; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 114. 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=Tfu_2361 {ECO:0000313|EMBL:AAZ56394.1}; OS Thermobifida fusca (strain YX). OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56394.1}; RN [1] {ECO:0000313|EMBL:AAZ56394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YX {ECO:0000313|EMBL:AAZ56394.1}; 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; AAZ56394.1; -; Genomic_DNA. DR AlphaFoldDB; Q47MC8; -. DR STRING; 269800.Tfu_2361; -. DR KEGG; tfu:Tfu_2361; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. 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 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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:AAZ56394.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ56394.1}; KW Transferase {ECO:0000313|EMBL:AAZ56394.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394..416 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 39..302 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 419 AA; 45239 MW; 0308554DF39495B2 CRC64; MSIEQPPTER PKADVTGRRP SVTVDGQASG SERVLAGRYV LREPIGRGGV GTVWRATDLV LDREVAIKEL RLPDDVTEDE RNSLLRRTTR EARVAGRLSH PNVVTVLDVV NEDGRPWIVM ELVEARTLAE IIDIAGPLPY PRVAEIGLQL ISALKAAHDE GIVHRDVKPE NVMISEDGRV VLTDFGLAAW TGESALSSSG RIIGSPSYLP PERAKAGPVG PASDLWSLGA TLYAAVEGHP PYGRKGYIAI LRGDDVEEPP PAANAGPLAP VLAGLLKVDP NERLTAESAT AMLRIASLAP WAPETSPETA ARMAEAVRRQ QEREKLSAVD HFRAGAEVLR TNLQEQVSHV SDALQRHRPE SVSALLTAIR ESTDALGLTS SGKHRSKRSR KKQAVIVAGV GLFVLLLLSV VLWALVFRT //