ID A0A167GDU6_9GAMM Unreviewed; 818 AA.
AC A0A167GDU6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ANB16452.1};
GN ORFNames=I596_415 {ECO:0000313|EMBL:ANB16452.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB16452.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB16452.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB16452.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) 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; CP015249; ANB16452.1; -; Genomic_DNA.
DR RefSeq; WP_067643394.1; NZ_CP015249.1.
DR AlphaFoldDB; A0A167GDU6; -.
DR STRING; 1300342.I596_415; -.
DR KEGG; dko:I596_415; -.
DR PATRIC; fig|1300342.3.peg.403; -.
DR OrthoDB; 9783151at2; -.
DR Proteomes; UP000076830; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ANB16452.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076830};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ANB16452.1};
KW Transferase {ECO:0000313|EMBL:ANB16452.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..301
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 795..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 818 AA; 87964 MW; 38C0C0CCC5C5C3AB CRC64;
MTHRARDLLE PGVLLGGALL RDLLARSDTE ALPAGTRLGA YRVVRELGRG GMGVVHLAER
ADGEFAQQVA LKCLAERGSA AGTELFRRER QILAGLRHPN IARLLDGGSD AEGLLWFAME
WVEGERIDRH CRRHGLSLDA RLRLWLGVAE AVQFAHARLL IHRDIKPGNV LVDADGRPRL
LDFGIAVLLG DGDSPRAYSP GHASPEQLAG EAVGTASDQY QLGRLLAGLL VRDGDGDATA
TGLGDGTPPA AAPPSLHAAH WIAMPAVRRR ELLAVLGRAC AADPAARYGS VTELRADIER
LRERRPVEAL RGRWPYVLAC ALRRRPVTAI AVTLAGLAAI ALVLAFNARL ARERDLARAE
AAKVRAINAF VSDDLLAAAD PFTASQPDLR VREALDRALA RVGRRFADQP AIESELRRTL
GATYAGIGEL GLAGEQFDRA YALRRRLAPA DDPDAVGIVL QQARRDLAAS DYAAAQHRLE
TLIGVLEARR DGGGDALIAA RIALLDTLSW AGRLDEAVTL DATLVQALQT RPDDDALKLD
HADTRGHLWL LQGHAEPAAA LFDATAARRA ARDGADDYRR LRSLEGKARA LRDGGRQAEA
IAVLRDLHAR RLAVFGTEHP ETLRNHNELA VALSQSGDRA AAIAIWTGDL AIKQRRLGPG
HASTLSTRYN LANELLASRR YAEAETAFRA LLEAERAARG ADDPGAWITQ MSLANAIGRQ
DRPAEALGLL DALLDDPAAL GGRPERAIAL VYRSRTRTAL GRSDAALADA RAAVAAFEAT
VGTDHRRTAQ AREWLASLEA PAAPDRTGSS DARTPRER
//
