GenomeNet

Database: UniProt
Entry: E6ZI14_DICLA
LinkDB: E6ZI14_DICLA
Original site: E6ZI14_DICLA 
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}.
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; 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
//
DBGET integrated database retrieval system