UniProt: Q7ZXU6

Database: UniProt
Entry: Q7ZXU6_XENLA

LinkDB:  Q7ZXU6_XENLA 
Original site:  Q7ZXU6_XENLA

All links

Ontology (5)   
   GO (5)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (22)   

Download RDF

ID   Q7ZXU6_XENLA            Unreviewed;       404 AA.
AC   Q7ZXU6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   Name=pdk4.L {ECO:0000313|RefSeq:NP_001080097.1,
GN   ECO:0000313|Xenbase:XB-GENE-866081};
GN   Synonyms=3j828 {ECO:0000313|EMBL:AAI10981.1,
GN   ECO:0000313|RefSeq:NP_001080097.1}, pdk4
GN   {ECO:0000313|RefSeq:NP_001080097.1,
GN   ECO:0000313|Xenbase:XB-GENE-866081}, PDKe
GN   {ECO:0000313|RefSeq:NP_001080097.1}, PDKk
GN   {ECO:0000313|RefSeq:NP_001080097.1}, xPDKe
GN   {ECO:0000313|RefSeq:NP_001080097.1}, xPDKk
GN   {ECO:0000313|RefSeq:NP_001080097.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH44112.1};
RN   [1] {ECO:0000313|RefSeq:NP_001080097.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH44112.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH44112.1}, and Heart
RC   {ECO:0000313|EMBL:AAI10981.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001080097.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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; BC044112; AAH44112.1; -; mRNA.
DR   EMBL; BC110980; AAI10981.1; -; mRNA.
DR   RefSeq; NP_001080097.1; NM_001086628.1.
DR   STRING; 8355.Q7ZXU6; -.
DR   PaxDb; 8355-Q7ZXU6; -.
DR   DNASU; 379789; -.
DR   GeneID; 379789; -.
DR   KEGG; xla:379789; -.
DR   AGR; Xenbase:XB-GENE-866081; -.
DR   CTD; 379789; -.
DR   Xenbase; XB-GENE-866081; pdk4.L.
DR   OMA; EIVICQG; -.
DR   OrthoDB; 3058550at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 379789; Expressed in heart and 18 other cell types or tissues.
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:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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:SF15; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE ISOZYME 2, MITOCHONDRIAL; 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   2: Evidence at transcript level;
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};
KW   Pyruvate {ECO:0000313|RefSeq:NP_001080097.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          242..365
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   404 AA;  46023 MW;  2572BE084076DC31 CRC64;
     MKFARFLLKN AALANAPKQI ERFSRFSPSP LSMKQFIDFG SANGCEKTSF GFLRQELPVR
     LANIMRELYI LPDQLLGTPS VQLVQSWYIQ SLMELIEFVE RDPEDQRVLS DFTEALVTIR
     NRHNDVVPTM AQGVIEYKEA FGVDPVTNQN VQYFLDRFYM SRISIRMLIN QHTLLFDGGT
     NPAHPKHIGS IDPNSDVVEV VHDAFDTAKM LCEQYYLASP ELRIKQANGK DPSQPIHIVY
     VPSHLYHMLF ELFKNAMRAT IENHETSPRL PPIKVNVVLG SEDLTIKISD NGGGVPLRKI
     ERLFSYMYST APRPLMDNSR NAPLAGFGYG LPISRLYARY FQGDLMLHSM EGFGTDAVIY
     LKALSSESVE RLPVFNKSAW KHYKFCTEAD DWCIPSSEPK NLAR
//

DBGET integrated database retrieval system