ID   I2H5Y3_TETBL            Unreviewed;       496 AA.
AC   I2H5Y3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   Name=TBLA0F02450 {ECO:0000313|EMBL:CCH61785.1};
GN   ORFNames=TBLA_0F02450 {ECO:0000313|EMBL:CCH61785.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH61785.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH61785.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806321; CCH61785.1; -; Genomic_DNA.
DR   RefSeq; XP_004181304.1; XM_004181256.1.
DR   AlphaFoldDB; I2H5Y3; -.
DR   STRING; 1071380.I2H5Y3; -.
DR   GeneID; 14496894; -.
DR   KEGG; tbl:TBLA_0F02450; -.
DR   eggNOG; KOG0787; Eukaryota.
DR   HOGENOM; CLU_023861_1_1_1; -.
DR   InParanoid; I2H5Y3; -.
DR   OMA; ICEAQEH; -.
DR   OrthoDB; 3058550at2759; -.
DR   Proteomes; UP000002866; Chromosome 6.
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; 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   SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
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:UP000002866};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          77..238
FT                   /note="Branched-chain alpha-ketoacid dehydrogenase
FT                   kinase/Pyruvate dehydrogenase kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10436"
SQ   SEQUENCE   496 AA;  57936 MW;  24B1EA9BD0A58075 CRC64;
     MKFSNGVLRN APYPPYRLNP PDFTKYCPVR PINEALAPYV NETLQAYNRR SKYVNKHHYY
     HNRTVLVKEY LTKDPHPVSL NQLSQYYDDS SRLTKQKIIS SGVFVKEELS IRLAHQLNML
     QQLPYNVVNN FHFNQVYESY YNMFERIRRM PGILTIEENA IFTRMLIKIL HDFNSLNLPH
     LIMGALECMI LGLYPSNKMD ELVSYLLRAR ISRRIIAEEH ISITENFSKG KTKNATIFGD
     IFQKCSAEYY LKKAALQAQR FIGDMYFPTI PMPEFKIEGD TDLSFYFLPN HITYLLGEIL
     RNTYEATIKE YIRSGSSKPS PITVTVISNK DFIIFRISDL AGGVHLDENQ LWSFGKSKEK
     AKKSLDNFHK LPGLQTISIY DHLYDKKSIS RKEYKKIQTN YYYSSLTPMG YVNPWHKDQN
     RSDITTEGFN MNRPLLGLFE RSFRYKLGIG LAMCKVYADY WNGDVQLHSM EGYGTDTVLK
     LRHLTNYSNV PQLDKL
//