ID   Q10Z84_TRIEI            Unreviewed;       662 AA.
AC   Q10Z84;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Serine/threonine protein kinase with TPR repeats {ECO:0000313|EMBL:ABG52440.1};
GN   OrderedLocusNames=Tery_3337 {ECO:0000313|EMBL:ABG52440.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG52440.1};
RN   [1] {ECO:0000313|EMBL:ABG52440.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG52440.1};
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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP000393; ABG52440.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q10Z84; -.
DR   STRING; 203124.Tery_3337; -.
DR   KEGG; ter:Tery_3337; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_407636_0_0_3; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABG52440.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABG52440.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABG52440.1}.
FT   DOMAIN          10..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          287..320
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          388..421
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          569..602
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   662 AA;  74778 MW;  AF77FB7395510644 CRC64;
     MGTLLKQGWY KIEKVLGQGG FGITYKAIYC LNSTLVAIKE LWPESGYRHD KSVVWPPSIA
     PIDQKEQVEK FKLEAAYLQR CNSPNIAKVY DCFEENSSIY MVMEFIDGVS LSSLMVNQKC
     LHENKVIEYA KQIANALVVV HENNLLHRDI KPENIMIDSS DRAVLIDFGT AREFIAGKTG
     DLTQLLTPGY APFEQYSKNS KRYAASDIYA LCASMYELLT GELPSGAVER ATAFSGGAPD
     PLLPPRQINS LISPHLEKVI LMGMRFRVEE RIQTAEELIN AFDGKLVSPL HQKAKDYVSK
     GDLNNAVSTY ETCLEREPDN GEATVELALV LVYMDEDRAV TVAQKGMQLK PQDGRSYGVC
     GLVGCHRRQW NHAAQQLEQG IRLSPKEAWI HANLAWALGQ QGNWESAERT IQQGLQLDPN
     STFALGLKAW ISFHKKQWRF VIQAGTQAIF KSQQEGSRIA MALQAWVYPF TIAALDKVTT
     KKGGDVKRRL RNFVVQVPNN SIALGFQAWY EYRDRNLNAC RQSLELACKC GDIPNWVARD
     RGLIDEHLND LPSALEWYKH RHQEIPQDAW ICYRLGTVLA RLNQWQDAKG YLEQAVKQDP
     NLAPAYRNLG WVLSNLLTVD GKIQSVQDLM AAYRQALALY EVQDMNEAQQ IRAMFQAIDI
     LL
//