ID A0A091KNU2_9GRUI Unreviewed; 379 AA.
AC A0A091KNU2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
DE Flags: Fragment;
GN ORFNames=N324_01345 {ECO:0000313|EMBL:KFP42269.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP42269.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP42269.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP42269.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK752654; KFP42269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KNU2; -.
DR Proteomes; UP000053330; 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 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 InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947:SF21; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE ISOZYME 3, 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; 1.
DR PROSITE; PS50109; HIS_KIN; 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:UP000053330};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 211..335
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 356..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP42269.1"
FT NON_TER 379
FT /evidence="ECO:0000313|EMBL:KFP42269.1"
SQ SEQUENCE 379 AA; 43497 MW; 80D16267A24CFFB7 CRC64;
SVFSFLLTGR DNACEKTSYM FLRKELPVRL ANTMREVNLL PDNLLNRPSV GLVQSWYMQS
FLELLEYENK SPEDPHVLDD FLDVLIKVRN RHNDVVPTMA QGVIEYKEKY GFDPFVSSNI
QYFLDRFYTN RISFRMLINQ HTLLFGGDIN PAHPKHIGSI DPNCNVAEVV KDAYETAKML
CEQYYLVAPD LEVEEFNAKA PNKPIQVVYV PSHLFHMLFE LFKNSMRATV ELHEGKREVY
PSIKTLVTLG KEDLSIKISD QGGGVPLRKI DRLFNYMYST APRPSLEPSR AVPLAGFGYG
LPISRLYARY FQGDLKLYSM EGVGSDAVIY LKALSSESFE RLPVFNKSAW RHYKTTPEAD
DWSNPSSEPR DASKYKANR
//
