ID A0A182YN09_ANOST Unreviewed; 466 AA.
AC A0A182YN09;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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};
OS Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI09845-PA, ECO:0000313|Proteomes:UP000076408};
RN [1] {ECO:0000313|Proteomes:UP000076408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA Sharakhov I.V., Tu Z.;
RT "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT stephensi.";
RL Genome Biol. 15:459-459(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASTEI09845-PA}
RP IDENTIFICATION.
RC STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI09845-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182YN09; -.
DR STRING; 30069.A0A182YN09; -.
DR EnsemblMetazoa; ASTEI09845-RA; ASTEI09845-PA; ASTEI09845.
DR VEuPathDB; VectorBase:ASTE009652; -.
DR VEuPathDB; VectorBase:ASTEI09845; -.
DR VEuPathDB; VectorBase:ASTEI20_037331; -.
DR OMA; NEMPSIC; -.
DR Proteomes; UP000076408; 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:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16929; HATPase_PDK-like; 1.
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:SF3; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; 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; 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:UP000076408};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 269..425
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 466 AA; 53295 MW; 99382DB0F7CDE371 CRC64;
MKLFPVRLSN INKMLDFYSQ FNPSPLSIKQ FIDFEKKNAQ MFTKDSVPGL FITKQNNSSC
CIPAGLNACP RKSFVFLRKE LPVRLANIMK EITLLPESLL RMPSVGLVSA WYVKSFEEVL
AFEKTDPTDP NLEKYWQLLE FCKSLIQIRD RHSDVVQTMA QGILELKESR DGAIEPSTEL
SIQYFLDRLY MSRISIRMLI NQHTILFGEI PQTGRHIGSI DPLCDPHMVV RDAYENARFL
CDQYYLASPE LEVIEHNEID KGNPIKIVYV PSHLYHMLFE LFKNSMRAVM EHHGTENDVP
PIKVTIVKGK EDICVKMSDQ GGGIARSQVD QLFKYMYSTA PQPPKSKTDL PLVPLAGMTQ
IADLLAYYVI IKHLFFVPYF QQMAIGYGYG LPISRLYARY FHGDLVLFSC EGYGSDAIIY
LKAFSDEANE LLPIFNKTST RFYKATVPTG DWSNQVKGKK TKPIVI
//
