ID   Q47N61_THEFY            Unreviewed;       548 AA.
AC   Q47N61;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Tyrosine protein kinase:Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ56108.1};
GN   OrderedLocusNames=Tfu_2075 {ECO:0000313|EMBL:AAZ56108.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56108.1};
RN   [1] {ECO:0000313|EMBL:AAZ56108.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ56108.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000088; AAZ56108.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47N61; -.
DR   STRING; 269800.Tfu_2075; -.
DR   KEGG; tfu:Tfu_2075; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_496885_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
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:AAZ56108.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ56108.1};
KW   Transferase {ECO:0000313|EMBL:AAZ56108.1}.
FT   DOMAIN          24..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   548 AA;  60217 MW;  BD06E30646D96D90 CRC64;
     MPHGFPSDLP PLHPSDHAIR IPGYDLVGRL GSGGMGVVYA ALDPQGRRVA VKLMRTEMVP
     DISQQRRRFQ EEVRALQRLR DKHVVPLLDS GIAAGRPWLA TAYVPGRNLQ QCGKLSGQRL
     FLLARGVAAA LCAIHRAGIV HRDLKPSNIM VYSDGTPVVL DFGIARSLGA AGLTGTGAPP
     VGTAGTISPE RYRGVSAPPA DVFAWGCVVV FAATGQLPFT APSPEEVMHR VLHSPPELHG
     FRGPLADLAV RAMAKNPAER PTAEQLLKEL DALGSPRPFA MPRVSRKTGD AATLLVLEMQ
     QHYANPVPWL RRNQERILGE ARRMGADRGL RDLVHRAAEA RLRAAELDEA LAEIASLLAP
     HERPRYRGYP VDEDGLVALA SGGAREQALL RRLLGERSVI VEKYAAQHIC RHVLCVSKHF
     GRGCRVLRRL RSQVVAVVDR TWEPLRELRH QIWAEHDALG HPRILLPPDQ ELVDRVYATA
     LLVRRRTDEL DRHRKAVLAL QCPTCWWASQ QEAVVQADPN TDKGLAHVVI ASVAADTARR
     FAEAVRQG
//