ID   Q5YRU1_NOCFA            Unreviewed;       942 AA.
AC   Q5YRU1;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:BAD59100.1};
GN   OrderedLocusNames=NFA_42510 {ECO:0000313|EMBL:BAD59100.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59100.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD59100.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59100.1,
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; BAD59100.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YRU1; -.
DR   STRING; 247156.NFA_42510; -.
DR   KEGG; nfa:NFA_42510; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_311655_0_0_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:BAD59100.1};
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:BAD59100.1};
KW   Transferase {ECO:0000313|EMBL:BAD59100.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        726..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          298..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..370
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..429
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..518
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..673
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..720
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   942 AA;  94755 MW;  60B3376D0B3EBC2F CRC64;
     MFAGFTVERL LGQGGMGSVY LARHPRLGKL TALKLLNPEL FTDRQVRARF DREADLAAQL
     DHPGIVAVYD RGSENHQLWI SMQYVDGVDA ASVNPLTLPP ERAVQIIEGV ADALDYAHGR
     GVLHRDVKPG NILLARASAG QGERVFLSDF GIARLREDTT HLTQTGMFTA TLAYASPEQM
     TGAPLGNRSD QYSLACALYW LLVGVGPFDA ANPADIIHGH LNLAPVPVSV RRPGLNPALD
     AVLAAGLAKH PDHRYRTCTE FATAARKALT ATGAPPLPTP YPPGHPYPGA QAFPAPGGVP
     VGHAPAAPGG HAVPPGGVPA GPNGPGGFPP GGAPMPVPGA AGPVPPGAAP AGPAPGVPGQ
     PAPGGPAQPA PGVPGQLASG VPAQPVPGVP AQPAPPASGQ PALGVSGQPV PGVPAQPVPG
     APVQPTPGDP SQSAPLAADQ HAPAVPAQPA PGVPGEVGPD VSAQPAPGGP AQPAPTPTGG
     PVGQQGGAGP VPPGAGGPDA APPAPASMPA PAPAPDSPPG AASGTAVPSA ADALPAQGDS
     SIPTDTDVAR SETVPHHEVR GGPPREPADA ARPGTAEPAS AAADRPARVS LHKDATTDIG
     GTEQDSDGVE REEIVSAGQA RASAAPSSDP ALGATASPSA ADAADSAGGA RSPHEDDPPA
     GLRDDDHGGE RDAARTEVLV EAVRRPRPAG WQAPGAGAPP PPGGFSGPPP YPPPAHPPRP
     RSAWRWVAPV VLGVVAVLVL AVGAVAVLLL SGEPDTESAA DSAQPPGPTR SMSGDPFAQS
     RRAFPGLLPQ GTETEGPGYG DTTCIALRRG QNLRIDDEIL AGGPWLVAWE CRAGAGSADG
     VDYTILHYDS SATARDTIED LPTAVGLTGR KDGVPYTQHA WVDRDSRQSL DYTAKLVVAF
     PTDATRAPYL LYASHHGASR HPMATLPSAD EELGAWWASA PL
//