ID   Q110S1_TRIEI            Unreviewed;       593 AA.
AC   Q110S1;
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:ABG52003.1};
GN   OrderedLocusNames=Tery_2829 {ECO:0000313|EMBL:ABG52003.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG52003.1};
RN   [1] {ECO:0000313|EMBL:ABG52003.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG52003.1};
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000393; ABG52003.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q110S1; -.
DR   STRING; 203124.Tery_2829; -.
DR   KEGG; ter:Tery_2829; -.
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; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:ABG52003.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABG52003.1};
KW   Transferase {ECO:0000313|EMBL:ABG52003.1}.
FT   DOMAIN          11..308
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          275..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   593 AA;  66654 MW;  4587F90B2F857C06 CRC64;
     MQSEQILRNR YKVIKSLGTG GFGYTYLAED LDLPGYPKCV VKHLKPKSPD STVLNIARKL
     FLREADILYK LGNDSDQIPR LFAYFQEQRE FYLVQEYIEG QDISRELTPG KKLSESDTIA
     LLKGILEALT VAHQNNVIHR DIKPQNLMRR RSDNKIVLID FGAVKEIDVL TINQQGATTL
     TVAVGTPGYM PSEQSNGKPK LSSDIYAVGM VGIRALTGKE PQSLLTDPKT GNVIWRNEAQ
     VSNRLADILD KMVHEYFPQR YENAMEVLDV LQEARKKPNP PKPTQRPAAE STLNVNPSQP
     RGQGGSWFAG RFFNQKPAKI SIQTFTTVTV NRRGEIISRA QGQAEVITEN IGNGVSLEMV
     KIPGGRFLMG SPKKEAERLD KEGPQHYVDV PEFLMGKYAV TQAQWEAVMG NNPARFKGAN
     RPVEKVSWND ATEFCRKLSR ITGKQYSLPS ESQWEYACRA RTTTPFYFGE TITPELVNYD
     GNYTYADAPK GKYRKETTDV GIFPPNAFGL YDMHGNVYEF CQDVWHENYN GAPTDGSAWE
     TGGDSSRRVC RGGSWVNYPG RCRSADRINY DSVGADYIGI GFRLVSFPPR TFE
//