ID A0A1S3IMW8_LINUN Unreviewed; 427 AA.
AC A0A1S3IMW8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=LOC106165756 {ECO:0000313|RefSeq:XP_013399547.1,
GN ECO:0000313|RefSeq:XP_013399548.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013399547.1};
RN [1] {ECO:0000313|RefSeq:XP_013399547.1, ECO:0000313|RefSeq:XP_013399548.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013399547.1,
RC ECO:0000313|RefSeq:XP_013399548.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_013399547.1; XM_013544093.1.
DR RefSeq; XP_013399548.1; XM_013544094.1.
DR EnsemblMetazoa; XM_013544093.1; XP_013399547.1; LOC106165756.
DR EnsemblMetazoa; XM_013544094.1; XP_013399548.1; LOC106165756.
DR GeneID; 106165756; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000085678; Unplaced.
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: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; 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 Pyruvate {ECO:0000313|RefSeq:XP_013399547.1,
KW ECO:0000313|RefSeq:XP_013399548.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 252..376
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 427 AA; 48639 MW; 3EEF1FBB053481D0 CRC64;
MMKSALLRPT RPLGFVRRFR CQPAAISVVK KYAEFNPAPL SLRNLLDFGQ NPCQQKSFKF
LRFELAVRLA NMLKEIEELP KDLMNTSSAD LVHRWYEESF RELMEFENAS SSDQSVLSEF
SEALEKIRSR HSTVVETMAQ GVMELANSSP DGVLEDATRK DIQYFLNRFY ISRISIRMLI
NQHILLFGNQ LNQERRYIGS IDPHCDVLEV VQGAYEDAKG LCDLHYCITP KLDIKCFNPY
EQGEPIQMVY VPSHLHHIMF ELFKNSMRAT IETRSNVTDS DLLPHIEVKI FKGKEDITIK
ISDQGGGFSR DQLDLMFNYT YTTASKPSAD HHTPFAGYGY GLPLSRLYAV YLNGNLDLAP
VEGHGTDAYV YLKTLSQAAS ELLPVFNKTT AKYYNSPIPV ADWSNPSHTT GLTTFLSRTY
CTKTSNQ
//
