ID   Q47SC8_THEFY            Unreviewed;       360 AA.
AC   Q47SC8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ54639.1};
GN   OrderedLocusNames=Tfu_0601 {ECO:0000313|EMBL:AAZ54639.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54639.1};
RN   [1] {ECO:0000313|EMBL:AAZ54639.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54639.1};
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};
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DR   EMBL; CP000088; AAZ54639.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47SC8; -.
DR   STRING; 269800.Tfu_0601; -.
DR   KEGG; tfu:Tfu_0601; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_061762_1_0_11; -.
DR   OrthoDB; 9788659at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; PTHR24349:SF243; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE IV; 1.
DR   PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 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   Kinase {ECO:0000313|EMBL:AAZ54639.1};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ54639.1};
KW   Transferase {ECO:0000313|EMBL:AAZ54639.1}.
FT   DOMAIN          8..292
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          315..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   360 AA;  40152 MW;  7CE030AD3F3AC74A CRC64;
     MSEFIGKYRI ITDFTTSGGG QCRWAFAVHG GKEYFIKEFL SPTYPLPDSP GSKATKERKL
     RKCEQFEKHH REITKTLKRL SKPGGNLVIT QDFFRHGAKY YKVTEKIDTS ALSLEEIAAE
     PMERRLLMLI TVTHSLKILH QAGLVHGDIK PENILIKGTV KNYHTAKLID FDNAFFSGKP
     VPPDDMVGDL NYYSPETFGY LNGTVMGEQL TTASDIFALG LVAVQFLTGS LVSFIPVEGA
     GRYPGELCAA GASYTTGLEE IFPQADSFVR KMLSAEPSKR PTVDQVFDHV KELRSEVKKR
     EDFITTTIVP RASSAKKSRL KGTLLKKSAS TSREAEPTPR NEKRSRLRGT LLEKRDSPPA
//