ID   Q72IX6_THET2            Unreviewed;       253 AA.
AC   Q72IX6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=TT_C1005 {ECO:0000313|EMBL:AAS81347.1};
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS81347.1, ECO:0000313|Proteomes:UP000000592};
RN   [1] {ECO:0000313|EMBL:AAS81347.1, ECO:0000313|Proteomes:UP000000592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27
RC   {ECO:0000313|Proteomes:UP000000592};
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Overbeek R., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(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};
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DR   EMBL; AE017221; AAS81347.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q72IX6; -.
DR   KEGG; tth:TT_C1005; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_0_0; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; 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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43895; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE KINASE-RELATED; 1.
DR   PANTHER; PTHR43895:SF168; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AAS81347.1};
KW   Protease {ECO:0000313|EMBL:AAS81347.1}.
FT   DOMAIN          12..253
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   253 AA;  27883 MW;  ED49AFF59FD3A744 CRC64;
     MSLVGKTLSG RYRVVRPLAR GALARVYLAF DPFGTPYALK LFPPKARPRR DRELWVGRRL
     AHPNLNPVLE ALDLEEGPAL LLAYAPGEEL GRWMGKSPAF SQAMRVFHQL LLALAHMHEK
     GLVHRDVKPE NILVNAGEAR LLDFDLSGPA QERFQKPLLL GTPAYLAPEL LRGLPSGPEA
     DVYAAGIILY WMLTGEHPFA DPSGRVSLDP DRGPHPPVAG LGEEAALYLE RLLAPDPKAR
     FPTAQEALKA FPF
//