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Database: UniProt
Entry: Q6CUD8_KLULA
LinkDB: Q6CUD8_KLULA
Original site: Q6CUD8_KLULA 
ID   Q6CUD8_KLULA            Unreviewed;       473 AA.
AC   Q6CUD8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=KLLA0_C05654g {ECO:0000313|EMBL:CAH01302.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH01302.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAH01302.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382123; CAH01302.1; -; Genomic_DNA.
DR   RefSeq; XP_452451.1; XM_452451.1.
DR   AlphaFoldDB; Q6CUD8; -.
DR   STRING; 284590.Q6CUD8; -.
DR   PaxDb; 284590-Q6CUD8; -.
DR   GeneID; 2892383; -.
DR   KEGG; kla:KLLA0_C05654g; -.
DR   eggNOG; KOG0787; Eukaryota.
DR   HOGENOM; CLU_023861_0_0_1; -.
DR   InParanoid; Q6CUD8; -.
DR   OMA; RYIPQHI; -.
DR   Proteomes; UP000000598; Chromosome C.
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   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   PANTHER; PTHR11947:SF25; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR   Pfam; PF10436; BCDHK_Adom3; 1.
DR   Pfam; PF02518; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          72..228
FT                   /note="Branched-chain alpha-ketoacid dehydrogenase
FT                   kinase/Pyruvate dehydrogenase kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10436"
FT   DOMAIN          286..458
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
SQ   SEQUENCE   473 AA;  54663 MW;  CB46733E73EF934D CRC64;
     MSRNSVVRKV LDISQVPDFS RYSATRSINE LAPYISSTLS AYPTESKYIN QYHYYHNDNV
     LVKKYLQKKP HPMSLKQLAQ YYDDSSKLTK MKIISSGKFV KEELCVRIAH KLDLLQNLPF
     DVVNNFHFNQ VYESYYNIFE RFRKFPEIKD EKDNLKFCQF LHAILSDFNS LNLPHLIMGA
     LECRILDLYP QDKMDALISD LLRARISRRL IVEEHLSITS NYLSGKKENT LVLGDIFQKC
     NAKEYLNGAR EVCEAYINNM YFAGIKMPEL IINGDTELEF YFLPSHLKFL LGEILRNSYE
     VTVKETIRLG LEKAPPVTVT IISNDQSYLF RISDRGGGVP HSDKQIWSFG KSKELAKQSL
     DNFHHLPGLQ TLSLYDSSNG AHLKSDRYRQ TSLDRMSENN LTKGKFKVGQ PLMELLKRSP
     RYKLGIGLAL CKVYAEYWNG DLTVHSIQGY GTDTVLKLGN LMRHTDKLQL DRV
//
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