ID G8JR19_ERECY Unreviewed; 508 AA.
AC G8JR19;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN OrderedLocusNames=Ecym_3076 {ECO:0000313|EMBL:AET38588.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET38588.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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; CP002499; AET38588.1; -; Genomic_DNA.
DR RefSeq; XP_003645405.1; XM_003645357.1.
DR AlphaFoldDB; G8JR19; -.
DR STRING; 931890.G8JR19; -.
DR GeneID; 11472087; -.
DR KEGG; erc:Ecym_3076; -.
DR eggNOG; KOG0787; Eukaryota.
DR HOGENOM; CLU_023861_0_0_1; -.
DR InParanoid; G8JR19; -.
DR OMA; RYIPQHI; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000006790; Chromosome 3.
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; 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:UP000006790};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 101..256
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
SQ SEQUENCE 508 AA; 59416 MW; 64F69763D1679454 CRC64;
MTLMSKNQQK IFMKRYMRGS RGVGRCERWQ KRYYSTTSGN ISQTPDFSKY FPTTPIAELT
TYISPTLSAY PRKSKYVNQQ HYYHNKEILI EKYLQRKPHA VSLKQLAQYY DDSNKLTKQK
VINSGQFAKD ELVVRMAHKL KQLQDLPFNV VNNFHFVQVY ESYYNIFERF RKFPAIRTLE
DNRRFAEFLC MILSDFNSLN LPHLIMGALE CRILDLYPQK QMDELISSFL RARISRRLIV
EEHLSVTSNY MSGKEENTLV LGDIIQNCSA KKYLLDASKM CENFIKDMFY DGIPLPEFII
DGDVDLNFYF LPTHLEYLLV ECLRNSYEAT IKQYIRLGLP KPHPIVVTVV ENENSFLFRI
SDRGGGILHD DKTIWSFGKS KELSMQSLEN FHKLPGVQTI SIYDHLYETD FNSSDLDLAF
GKLKYTSLQS MNETNLKKGR YKVNRPLLNL LGRPFRYKLG IGLAMCKVYA EYWNGDLTVH
SIQGYGTDTV LKLGNLMYHT DRLQLDKV
//
