ID W7U1N5_9STRA Unreviewed; 523 AA.
AC W7U1N5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=Naga_100124g14 {ECO:0000313|EMBL:EWM29718.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM29718.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM29718.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM29718.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036431};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWM29718.1}.
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DR EMBL; AZIL01000119; EWM29718.1; -; Genomic_DNA.
DR AlphaFoldDB; W7U1N5; -.
DR EnsemblProtists; EWM29718; EWM29718; Naga_100124g14.
DR OMA; IANDASQ; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000019335; Chromosome 2.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR11947:SF3; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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:EWM29718.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 355..516
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57839 MW; 1FA96E1BDA30E5D0 CRC64;
MIARHVQFLK TNLYQYASKR RFAQIATSST LFPHQSHLQQ HQQHGQGGAA GRSTPSFLQQ
QTLKADKLHT PTKIAGASVP WSNSAHNVSD SKSDILRDEE ATILSYAKKR SERVSLRSLA
EVGLGTRPWL SSLRDAMSLE NPLCSLNVRL CRVSDPHSPA QKGLLRMATF LHRELPIRFA
RGITFIDKLD SSRQAPSLRV VREWYRESFR DVVSSPCPVT DGCEESFVKV LTRVRDRHAD
ELLLVARGVF ELRAKLGMDA LDGRGGREAL HAQLDELHLK RIALRILVGH YLALHQPPRP
NYVGIICTRT KLQDVIETAA ADARWICKQR FDGCAPRVEV IGGEGMVMAC IPESLYYLSM
ELIKNSLRAV AERYNEALFR DGSMAHGAGG DEGCVPSIKV ILSREYSLTE GQQVVIEVRD
EGGGIPPEDL GKVFCYLFST AADADVQQLV MDRHASGLGG ERSKHNRGNS KKVPLAGLGY
GLGIAKSYAL YFGGELELKN RPGDGCSVFV TLSRLGECKE PLV
//
