ID   Q5YX79_NOCFA            Unreviewed;       602 AA.
AC   Q5YX79;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:BAD57212.1};
GN   OrderedLocusNames=NFA_23650 {ECO:0000313|EMBL:BAD57212.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD57212.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD57212.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD57212.1,
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; BAD57212.1; -; Genomic_DNA.
DR   RefSeq; WP_011208897.1; NC_006361.1.
DR   AlphaFoldDB; Q5YX79; -.
DR   STRING; 247156.NFA_23650; -.
DR   GeneID; 61133119; -.
DR   KEGG; nfa:NFA_23650; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000006820; Chromosome.
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:BAD57212.1};
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:BAD57212.1};
KW   Transferase {ECO:0000313|EMBL:BAD57212.1}.
FT   DOMAIN          15..266
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          294..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   602 AA;  62577 MW;  A9FD42DD250FF664 CRC64;
     MQPLGLDDPR RIGDYRLLGV LGAGGMGRVY LGRSAGGRTV AVKVIRPDLV ADPEFRTRFQ
     REVAAARRVG SSCTAPVLDA DVAANPPWLA TGYVAGLALS DAVERFGPLG EHSLLVLAHG
     LAEALIAVHA AGVVHRDLKP SNVLLALDGP KVIDFGIARA MDDTSLTTTG KVIGSPAFMS
     PEQVTGEPIG PAGDMFALGG VLAYAAAGQG PFGTGDTVQL LWRVVYEEPR IEAVPPRLRP
     AVAACLAKNP ADRPTPRQVL DQLTALGLPD RAGWLPAPVL EDVSARAVRL LDLDSEPDDG
     YGEPTRAATI PSGHGTAPSH PGTARYPQAD PYRQSSGYGT AAGQGTGAQP EPGRYGTTPT
     GWHTHTAHSG SDRSVDRNHH VPQDYSAHSP YGRQHGSGAG RTDATALHRP STAHEPSTRR
     SGRRGPLVAA LVVVGTAVAA GAFVIGTQLR DQPPHENAGA PPSAQVAEPT EAAPTTTAAT
     STTTAPESAV PAEFVGTWRG TAADGLVAFD IELVIDEGEI GAEVARSANT GKLIGQRCSR
     VERLTEANPQ QLTFVARLAD DSPRDCRDEG AVTTVRLQPD GSLAYSTPGL FGGSIAGILR
     RG
//