ID   Q117B6_TRIEI            Unreviewed;       617 AA.
AC   Q117B6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABG50408.1};
GN   OrderedLocusNames=Tery_1036 {ECO:0000313|EMBL:ABG50408.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50408.1};
RN   [1] {ECO:0000313|EMBL:ABG50408.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG50408.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG50408.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q117B6; -.
DR   STRING; 203124.Tery_1036; -.
DR   KEGG; ter:Tery_1036; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_012431_6_1_3; -.
DR   OrthoDB; 569031at2; -.
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; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR016187; CTDL_fold.
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   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   PANTHER; PTHR23150:SF37; FGE-SULFATASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABG50408.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABG50408.1};
KW   Transferase {ECO:0000313|EMBL:ABG50408.1}.
FT   DOMAIN          44..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   617 AA;  70235 MW;  FC8CB244C6591B47 CRC64;
     MRCLNCHTDG IPLETKICYN CGAYLPSLIR GLLTPGTQLG DKPYQIDYPL GRGGFGVTYR
     GHHTLLKQIV AIKEYYPQNY ALRHPTTGGF TIPRNQQEIF QQGLRRFLQE GKILAQLNHP
     HVVRVIDLFE ENETAYLVME LVRGKSLRKE LDSQPEKKFP PQKVKEIITD LVSALSAVHQ
     QGIFHLDIKP DNILLTPEGR LVLTDFGSAK QTFGTSMGTS STESFAESYA APEVLARGEV
     GVESDIFEVG MMVYEMLSGQ LPPNVLERSL SKEKSWEPEG LESSWQKLLM SALVLAKEGR
     PGNIEEWWEM NFHKKSTERT QESGWKTKEF KNRKKDISSP PRQKFGFEVI KVNSRGKEID
     RRSYEAEFLA ENLDSGLVLE MVYIPGGSFL MGSPEYEDER FDSESPQHQV NIKPFLMSKY
     PITQDQYQAI MGDNPSYFKG GKRPVERVSW HDATKFCEKL SSKTGKIYRL PSESQWEYAC
     RAGTSTPFYF GETMTSELVN YDGNYPYGNA PFGEYREQTT DVGSFLPNAF GLYDMHGNVS
     EWCLDAWHHN YYGAPTNGSA WKTGGSNRKR VLRGGCWDSY STNCRSAWRF YYNADDLYYY
     RGFRVVSSSP VVSAFNS
//