ID W6MNN4_9ASCO Unreviewed; 467 AA.
AC W6MNN4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=KUCA_T00004261001 {ECO:0000313|EMBL:CDK28279.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28279.1};
RN [1] {ECO:0000313|EMBL:CDK28279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28279.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28279.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; HG793129; CDK28279.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MNN4; -.
DR STRING; 1382522.W6MNN4; -.
DR HOGENOM; CLU_023861_5_1_1; -.
DR OrthoDB; 3058550at2759; -.
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 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 326..460
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 53151 MW; 343A0A76C3ED495D CRC64;
MSHGWKLTQS LREEIYKYAK FPPTGVSLRQ MVQFGPKPSA GTLFHASQFV VEELPIRLAH
RVKELEELPN DLNKVESIQL VRDWYAQSFE ELTSLPKPTI DESLRKLLYG NGNNNLYHPS
TNSNPPAEDE SATSTPLLFD DDGLIVRKST THKQSQYKQQ NQFLTTEDYI ATTKQKRYYI
PCPINETYPA EVYEYNRVVT DTLKVIKKRH DATVTTVAKG VQEWKHNTHV SLVDTNVQSF
LDRFYLSRIG IRMLIGQQIA INQDHSTFND DYVGVICLNT NVAEIAQDAI ESARFTCEEH
YGLMEAPQVQ LYCPTNLNFM YVPGHLVHML FETLKNSLRA TVEHHLKQNL DKDIEDIQFP
PVKIIVAEGE EDITIKISDE GGGIARSAMP LIWTYLYTTV EALPVEDPWG GKTDFRAPMA
GYGYGLPISR LYARYFGGDL KLISMEGYGT DVYLHLNRLS SSSEPLP
//
