ID   Q8DGU1_THEVB            Unreviewed;       488 AA.
AC   Q8DGU1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=tll2222 {ECO:0000313|EMBL:BAC09774.1};
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221 {ECO:0000313|EMBL:BAC09774.1, ECO:0000313|Proteomes:UP000000440};
RN   [1] {ECO:0000313|EMBL:BAC09774.1, 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=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; BA000039; BAC09774.1; -; Genomic_DNA.
DR   RefSeq; NP_683012.1; NC_004113.1.
DR   AlphaFoldDB; Q8DGU1; -.
DR   STRING; 197221.gene:10748833; -.
DR   EnsemblBacteria; BAC09774; BAC09774; BAC09774.
DR   KEGG; tel:tll2222; -.
DR   PATRIC; fig|197221.4.peg.2331; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3468; Bacteria.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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:BAC09774.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000440};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC09774.1};
KW   Transferase {ECO:0000313|EMBL:BAC09774.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        319..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          347..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..422
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..488
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  52554 MW;  71287B898A6DBB09 CRC64;
     MSMSSLGLLS VGTTLQGGKY HLDALLSQGG FGVTYRATHT LLHQPVVLKT LNLQQEPPKR
     IHDLGERFIQ EAQRLAQFNH PHIVRVSDCF IEGGRPFIVM DYIPGRTLAQ VIQEEGPLPE
     KTALHYIRQV ASALELVHEH GLLHRDVKPD NIMLREGTDQ VVLIDFGIAR EYTTGVTETN
     TGLVSAGYAP VEQYLPRHQW TPATDVYALA ATLYALLAGR PPVASILRDR VPLEDLRQFQ
     PNLSQRTIDA IEAGMALDVR ERPQTVRAWL QLLMGQSVAR QTTATVAVMP QHRSTVFAST
     QPEGTAVVAS PRQRNFSPWL WLLGTAVFGS LAGIGLGLFL RNQPVDTVTP PPPRPQEQEF
     PPTLPRVVPP VEVTPSPEPT PNPAPEPTPS PESTEPATPS PAPQEASPPQ PTPPPSSSEP
     SNATPSPEPG VSQSSPPPAP VESPVPTPPP SPAAETPPPP TNSQPTSEPP TPPPQPTPPP
     SSSEPATP
//