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Database: UniProt
Entry: F4P5Y5_BATDJ
LinkDB: F4P5Y5_BATDJ
Original site: F4P5Y5_BATDJ 
ID   F4P5Y5_BATDJ            Unreviewed;       485 AA.
AC   F4P5Y5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=BATDEDRAFT_19998 {ECO:0000313|EMBL:EGF79509.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79509.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF79509.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) 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; GL882886; EGF79509.1; -; Genomic_DNA.
DR   RefSeq; XP_006679834.1; XM_006679771.1.
DR   AlphaFoldDB; F4P5Y5; -.
DR   STRING; 684364.F4P5Y5; -.
DR   GeneID; 18237446; -.
DR   HOGENOM; CLU_023861_0_1_1; -.
DR   InParanoid; F4P5Y5; -.
DR   OMA; ICEAQEH; -.
DR   OrthoDB; 3058550at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IBA:GO_Central.
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:UP000007241};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          122..280
FT                   /note="Branched-chain alpha-ketoacid dehydrogenase
FT                   kinase/Pyruvate dehydrogenase kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10436"
FT   DOMAIN          326..468
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
SQ   SEQUENCE   485 AA;  54604 MW;  5D0C8E6C5E0F5BB3 CRC64;
     MGCDATFAAR HLTARTSRPS TLSCSTYTVL HSSSSPSLQS RSSLKPLSSR HPSLASASIT
     TRVLSSNTVI PRCSSLYTQS SACTHRPLLQ QNRCFVSASS ASHSNFYHNR VLEKYVEQEV
     KRVTLRQLSV FGRNFNLEKV LRSANYIRTE LSVRLAHRIS RFQQLPFVVG TNPHIEFIYN
     LYWEAFETFR SMAPITTIEQ NRELCAIVQS LLNAHLVAIP ELALGIAQSE QHMTTQAADK
     FINETLRSRI GRRVLAEQHI ALSQVFDGTK EAQPDWIGIV NINCHARAAV DKCASLAGKL
     FRQAYNIEPP EVIIDGFEDA TFTYIPDHIE YILFELIKNS IRIYLYNHRH HCYPKPICTK
     LPPVRVTIGK SDTHIMFRIS DQGGGIKQSS LPKVWSYLND SSKKRYLEFD KLPIISQATK
     TESVSILPSC ALHLGLGLPM SRVYANYWGG NISMYSMEGY GTDVYVSISI GNQCENLFDE
     VPTDV
//
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