ID Q5YW74_NOCFA Unreviewed; 752 AA. AC Q5YW74; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 116. 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=NFA_27200 {ECO:0000313|EMBL:BAD57567.1}; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Nocardia. OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD57567.1, ECO:0000313|Proteomes:UP000006820}; RN [1] {ECO:0000313|EMBL:BAD57567.1, ECO:0000313|Proteomes:UP000006820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD57567.1, RC ECO:0000313|Proteomes:UP000006820}; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, CC cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}. 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; AP006618; BAD57567.1; -; Genomic_DNA. DR AlphaFoldDB; Q5YW74; -. DR STRING; 247156.NFA_27200; -. DR KEGG; nfa:NFA_27200; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_012667_0_0_11; -. DR OrthoDB; 4569664at2; -. DR Proteomes; UP000006820; Chromosome. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Kinase {ECO:0000313|EMBL:BAD57567.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006820}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000313|EMBL:BAD57567.1}; Transferase {ECO:0000313|EMBL:BAD57567.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 500..522 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 542..567 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 598..617 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 629..651 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 686..705 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 717..735 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 168..475 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 752 AA; 82126 MW; A31D5DE2409377BC CRC64; MAHPAARVSR ATAAASPPQS AGRGSPVADV VTRFAEAWRD ARTPPDLTAF LPDSPALRRV SLIELIKVDL AQRWRRHVEP KRLAQYVAEL PELRTWPLPP DLIYEEFHLR RQAGQPVDVA EYTATYPAQA QVLSELLTTD DYHSTLLAGP VEPAGLDELE PGTSVDDFDL MTSLGRGAFA RVFLARQRSM QRLVAVKISR DKSTEPQTLA QLDHRHIVRV FDQRVLPSSG LRLLYMQYVP GGTLFSVLER LRAHPAQARA RGGALLLDVI DEVLTGKGEI RPGESATRAE LAGLTWPETI AWLGRRLADA LDYADRCGVL HRDIKPANVL LTAEGEPQLA DFSISFGSTV TGASPVAYFG GSLAYMSPEQ LAAVHPDLPG TAADLDVRSD LYALAVMLWE LLTGHKPFGD DHVTGGDRTT LDGMLERRRR GPGALPYADL PPDCPAALRR TLARALDPDP DRRWPTGADM AQQFDVCLDA RARDLVDPPP RSARVRVRAW LHPIMACAIA IPNALAILYS YQHNRTLIID KLDAQTQQRF DQVALTTYGL CFLLGVVATN VLIAHLWSVS RGLRHGRHYD AATLAKARSD TLRLAQRNVL TCFVLWALAG IVVPLTVQVS GSSLPAQSYL HFFATQIVCG GIAMAYPYFL VSFYSVRCLY PMFVPHGGLG PADAAELDRL DRRGTAFLAV AAAVPLLGVA GATFIPPADL PAVIVPLRVL GVGSALAFVG VYWLFRMSER DLAALARVVG QR //