ID A0A024TT46_9STRA Unreviewed; 439 AA.
AC A0A024TT46;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-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=H310_09984 {ECO:0000313|EMBL:ETV97189.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV97189.1};
RN [1] {ECO:0000313|EMBL:ETV97189.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV97189.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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; KI913974; ETV97189.1; -; Genomic_DNA.
DR RefSeq; XP_008874435.1; XM_008876213.1.
DR AlphaFoldDB; A0A024TT46; -.
DR STRING; 157072.A0A024TT46; -.
DR EnsemblFungi; H310_09984-t26_1; H310_09984-t26_1-p1; H310_09984.
DR EnsemblProtists; ETV97189; ETV97189; H310_09984.
DR GeneID; 20087034; -.
DR VEuPathDB; FungiDB:H310_09984; -.
DR eggNOG; KOG0787; Eukaryota.
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 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:SF3; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE, 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 46..194
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 48045 MW; 1B49B8C6B57D5B40 CRC64;
MHLRAAGVGR RSPGATRRQV HATAAAMSSP LSRDDISAMA KTSPMPLTLQ QMKTFATNGP
ELRLKASAFL HNELQVRFAR AVVELSELPL GLNETPPVKM AIANYTMLLH DLAAMKTPTT
YEDDAIFTAR ITQMKQQGSN LVPMICGGLH AIKATPRVKN ALRLQDVQDD LNTRLDTFFL
SRIGIRMLIG QHSKVGGRVK LTNVQDIVNE AVSRASALCD TYCGPPPPVV VRVAKNGNAP
FMYVRSHLHH MVFELLKNSM RATVERHARL RSSDGLPKCP LHPRPRMNHH SPLLGFVIPD
LDTIDGVTIF PPAGAAGSAL PPITVVISQG AEDLTIKISD EGGGVPRSEW RNLWQYTYTT
ADVVDPAVFK GEVNFRDHFC GGGYGLPISR LFARYFGGEV TFLSLEGYGS SAFIQAHRLG
KQAELVPGHT NFTLQPLTF
//
