ID   Q8DGL2_THEVB            Unreviewed;       582 AA.
AC   Q8DGL2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027};
DE            EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027};
GN   OrderedLocusNames=tlr2304 {ECO:0000313|EMBL:BAC09856.1};
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221 {ECO:0000313|EMBL:BAC09856.1, ECO:0000313|Proteomes:UP000000440};
RN   [1] {ECO:0000313|EMBL:BAC09856.1, ECO:0000313|Proteomes:UP000000440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM M-273 / NIES-2133 / BP-1
RC   {ECO:0000313|Proteomes:UP000000440};
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}.
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DR   EMBL; BA000039; BAC09856.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8DGL2; -.
DR   STRING; 197221.gene:10748922; -.
DR   EnsemblBacteria; BAC09856; BAC09856; BAC09856.
DR   KEGG; tel:tlr2304; -.
DR   PATRIC; fig|197221.4.peg.2413; -.
DR   eggNOG; COG0515; Bacteria.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 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   3: Inferred from homology;
KW   Kinase {ECO:0000256|PROSITE-ProRule:PRU00159, ECO:0000313|EMBL:BAC09856.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000440};
KW   Serine/threonine-protein kinase {ECO:0000256|PROSITE-ProRule:PRU00159,
KW   ECO:0000313|EMBL:BAC09856.1};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00159}.
FT   DOMAIN          1..254
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10027"
SQ   SEQUENCE   582 AA;  65405 MW;  2F144EF24BC656A5 CRC64;
     MDLAGQGQYG QVYLAVNRES GDLVAIKVLS ERQLLTRGFL RELNFLLTLQ HPHVVGCQAI
     DYIRVHHSPQ VSRSLVMDYC AGGTLRSLLE QEQALPLTTA LRLTLDILSA LAYAHHRGIL
     HCDLKPENIL LEVTATGWQA KVSDFGVARL IEDVKGSGQT GSPAYMAPER FYGQTMPASD
     LYAVGILLYE MIVGDRPFHG TPAELMAAHL SRPYTLPEGL PFLVRSIIAK ALDKLPQRRY
     KSAAEMTMAV QLALEVIEAE HHQQPLLFSR SPAAVWLGEP QGFALPRLPQ QVASTATGFY
     GVVGDRLWAW QARETIPEAT AQWPLPPLPI QLYGSEVSAW LRINALPPQL FCIHDQLIPL
     DGHLPSTLNP LTIDARGYWW AETQIDSAAA ELQLHVQLIN GQGRRTLRCQ WHGRTFVDTL
     LLNRRYGAVI SRSQDPETAH PITHFQLFDR RGHWRLYTPL PAHLTLLTPA HHQPWQVAAF
     EDHPQQPLLV LLHLRPWRIQ RLGLRFRPQF LCATPWGYVV AGRHSLNLVT HSGEIVGTAE
     SEQEIDGLGF TGDRHLWLIR RQGSGCVIQT WDITTWDIHL IL
//