ID E6ZI14_DICLA Unreviewed; 408 AA.
AC E6ZI14; A0A8C4NY50;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=PDK2 {ECO:0000313|EMBL:CBN81698.1};
GN ORFNames=DLA_Ib05400 {ECO:0000313|EMBL:CBN81698.1};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN81698.1};
RN [1] {ECO:0000313|EMBL:CBN81698.1}
RP NUCLEOTIDE SEQUENCE.
RA Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT "Analysis of single nucleotide polymorphisms in three chromosomes of
RT European sea bass Dicentrarchus labrax.";
RL Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN [2] {ECO:0000313|EMBL:CBN81698.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1016/j.ygeno.2011.06.004;
RA Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT DNA of comparatively mapped BAC clones.";
RL Genomics 0:0-0(2011).
RN [3] {ECO:0000313|EMBL:CBN81698.1}
RP NUCLEOTIDE SEQUENCE.
RA Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT into their evolution and molecular function.";
RL Mar. Genomics 4:109-119(2011).
RN [4] {ECO:0000313|Ensembl:ENSDLAP00005055990.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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DR EMBL; FQ310507; CBN81698.1; -; Genomic_DNA.
DR Ensembl; ENSDLAT00005059424.2; ENSDLAP00005055990.2; ENSDLAG00005023763.2.
DR GeneTree; ENSGT01030000234646; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16929; HATPase_PDK-like; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947:SF43; PROTEIN-SERINE_THREONINE KINASE; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032}; Pyruvate {ECO:0000313|EMBL:CBN81698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694389};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 241..364
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 408 AA; 46504 MW; DF91AC5C8DBA125C CRC64;
MKFVRFIMKN AAMASVPKHI EHFSKFSPSP LSMKQFLDFG SINACEKTSF VFLRQELPVR
LSNIMKEINL LPDKLLTTQP VKMVQSWYIQ SLIEILEFLD KNPDDYKVLG EFVDALVTIR
NRHNDVVPTM AQGIIEYKET FPHDAVTNQN IQYFLDRFYM SRISIRMLIN QHTLIFDGSA
NPVHPNTIGS IDPLCQVGDV VQDAFHSAKM LCDQYYLCSP DLILQEMSNK KNLPISIVYV
PSHLYHMLFE LFKNAMRATI ETHENSNNLP PIQVMVSLGG EDMSIKVSDK GGGVPFRRIE
NLFSYMYSTA PAPQMGEHTR PPLAGFGYGL PISRLYAKYF QGDLQLYSME GHGTDAVIYL
KALSTDSIER LPVYNKTALK NYKVSQEADD WCIPSKEPLD LSNYKVAK
//