ID A0A0D2ESL9_9EURO Unreviewed; 440 AA.
AC A0A0D2ESL9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=PV05_02293 {ECO:0000313|EMBL:KIW57730.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57730.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW57730.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57730.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847318; KIW57730.1; -; Genomic_DNA.
DR RefSeq; XP_013318314.1; XM_013462860.1.
DR AlphaFoldDB; A0A0D2ESL9; -.
DR STRING; 348802.A0A0D2ESL9; -.
DR GeneID; 25324201; -.
DR HOGENOM; CLU_023861_0_0_1; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
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:UP000054342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 54..217
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT DOMAIN 267..414
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF02518"
SQ SEQUENCE 440 AA; 49818 MW; 58AB139FBC37AC72 CRC64;
MLQVPRFLRP RALHVNGCTA FPPCRRASSR GGSSPPPWRP ASTLDDWVDR PIRPISLRQL
FFFGRTLTES RLLSSANYVR MELPTRIAHR LREMQRLPYV VVTNPHLSLV YELYYKSFEN
FRRMPVIRTV EENENFCKVI GESLREHMAV IPNLVMGVLE CQELVSADTM DKFVQAMLRA
RISRRVIAEQ HLALTETFNS PWHVPQPSSE NEFVGEVLLR CNAKEIIERV GKFTQDICKS
SAGADPMVPE IKIQGHINAT FPYVLSHLEY IIGELLRNSV QAVMERYKDP SQPPPPIEVL
ICETPQHVVI RISDQGGGIP RDIMPFLWSF NKGPRSASRL ENFRDVPTLA ATMQEVRQLE
AAEEKPSGKI RDSSLSTLAS RAPDLRLGMG LPMSRVYAEY WAGGLELHSL EGYGVDAFLQ
ISKLGNQNEQ LTSRASIDAV
//
