ID   Q5YRU7_NOCFA            Unreviewed;       807 AA.
AC   Q5YRU7;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:BAD59094.1};
GN   OrderedLocusNames=NFA_42450 {ECO:0000313|EMBL:BAD59094.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59094.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD59094.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59094.1,
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; AP006618; BAD59094.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YRU7; -.
DR   STRING; 247156.NFA_42450; -.
DR   KEGG; nfa:NFA_42450; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
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; 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAD59094.1};
KW   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:0000313|EMBL:BAD59094.1};
KW   Transferase {ECO:0000313|EMBL:BAD59094.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        650..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          279..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..304
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   807 AA;  83379 MW;  3C1677FE8520752E CRC64;
     MDGPGRRVGT RFGPYELRSL LGKGGMGEVY EAFDTSRHRL VAVKLLADEL AKDPVYQERF
     RRESQAAARL AEPHVIPIHD WGVLDGVLFI DMRLVAGTDL RTMLHHTGPL EPERAVRLVE
     QVAAALDAAH ADGLIHRDVK PANILVTDAD FAYLADFGIA HTEGDSAITQ VGMAVGSYIY
     MAPERFDSGT VTGRADIYSL ACVLHECLTG AAPFPSASMN VLVKAHLSEP PPRASALRPG
     LPASIDAVIA RGMAKNPADR FASALEMTRA ARAALGMRDT AAPPRPGGPG GVAPAAPVPP
     APATGGVPVT TGTGPMFVVR APDPSRFGAK SEPTVAASVL PPESTGEMSV PAVIHPTAPT
     VVRPSEFEFS PLPTQEQAIV PPASGAIPQV RPFPDEHLYP ESQRYGSESV SAPMPAVPPV
     APSPVAPAPA AAAPRVAPPT VSTSAASPGP GGPVVAQDDP PAPAAQPYSD EHPSGTYPVT
     GRAPADEPVG YVGARAYSDT DRPAFTAPET TRYPVPPVPE VRQPAPETAR YDDPAAPATR
     ALHQPYPPHA FGPAGPHGGG HAAPDPHAAY DPGDPHGVQA YSAIPDDRDR YGHPDPYGGQ
     PGHHPDPYAG AEYAAPGEPY ADPRRDRHVQ PGYGDPHAYA APGPERGRAM ALPLLAALAV
     VLVLVAGGLV AWRMFGGGNT DTTASEGTVP VATTAARPTG AAPPPATSAR PTTTTTTRVQ
     LPAGAKTCGS TSSAPNGNAA AGNSVTSCPF AEEVRRAYAA EATPGTRAPQ TITAVSPVTG
     RSYTMTCVPD DGLVTCTGGE NAIVYVY
//