ID Q5Z3R9_NOCFA Unreviewed; 635 AA. AC Q5Z3R9; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 121. 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_800 {ECO:0000313|EMBL:BAD54922.1}; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Nocardia. OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD54922.1, ECO:0000313|Proteomes:UP000006820}; RN [1] {ECO:0000313|EMBL:BAD54922.1, ECO:0000313|Proteomes:UP000006820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD54922.1, 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 --------------------------------------------------------------------------- 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; BAD54922.1; -; Genomic_DNA. DR RefSeq; WP_011206609.1; NC_006361.1. DR AlphaFoldDB; Q5Z3R9; -. DR STRING; 247156.NFA_800; -. DR GeneID; 61130921; -. DR KEGG; nfa:NFA_800; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000006820; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; cd06577; PASTA_pknB; 4. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF03793; PASTA; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 4. 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}; Kinase {ECO:0000313|EMBL:BAD54922.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000006820}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAD54922.1}; KW Transferase {ECO:0000313|EMBL:BAD54922.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 331..352 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 357..423 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 424..492 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 493..559 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 560..631 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 294..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..551 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 305..322 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 635 AA; 67465 MW; C935D65F4C4CE94C CRC64; MTTPKNLSAR YELGEIIGFG GMSEVHKARD LRLSRDVAIK VLRADLARDP TFYLRFKREA QNAAALNHPA IVAVYDTGEA EIDGGPLPYI VMEYVDGETL RDIVRGKGPL PPRRAMEIIA DVCAALDFSH KHGIVHRDMK PANIMINRSG AVKVMDFGIA RALADSSNPM TQTAAVIGTA QYLSPEQARG ETVDARSDVY SVGCVLFEIL TGEPPFTGDS PVAVAYQHVR EDPRLPSHVH HGVPRELDSV VLKAMSKNPA NRYQTAAEMR ADLIRVLGGQ KPSAPMVMTD EDRTTFMGAD EPGPRTYRAV ERDDDTAEQE PAEPNSGRRT AYLAFGAAAV LAVAFALFWV LIGPGSKPDQ VAVPDLSNKS AQQAQDTLQR LGFTVAIQQK PDSKVAVGNV ISTQPLGGSR IDKGSTVTVQ VSSGPAQVQV PRLDGLSVQQ AEQELNAVGL RMDPNVERRE SSAQDLDKVI GTEPGAGARV DVDQAIVVWV GKGPEKVRVP SVVGQDISVA QPNLVDSAGF KIDIEEVASS RPKGEVVATS PAGGSSADRG STVTVQVSAG DEITMPTLVG LTPSQAVERL RQSGWTGNAG QINQATTGTF EAGSVGRILQ QQPQAGSSIS KTATITITVG TLGPP //