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Database: UniProt
Entry: B2G4U8_ZYGRO
LinkDB: B2G4U8_ZYGRO
Original site: B2G4U8_ZYGRO 
ID   B2G4U8_ZYGRO            Unreviewed;       498 AA.
AC   B2G4U8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   Name=Zr_KLLA0F27423g {ECO:0000313|EMBL:CAQ43607.1};
GN   ORFNames=Zrou_10p43 {ECO:0000313|EMBL:CAQ43607.1};
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956 {ECO:0000313|EMBL:CAQ43607.1};
RN   [1] {ECO:0000313|EMBL:CAQ43607.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 732 {ECO:0000313|EMBL:CAQ43607.1};
RA   Gordon J.L., Wolfe K.H.;
RT   "Zygosaccharomyces rouxii homologs of Saccharomyces cerevisiae chromosome
RT   III.";
RL   Submitted (FEB-2008) 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; AM989989; CAQ43607.1; -; Genomic_DNA.
DR   RefSeq; XP_002496783.1; XM_002496738.1.
DR   AlphaFoldDB; B2G4U8; -.
DR   GeneID; 8204039; -.
DR   KEGG; zro:ZYRO0D08052g; -.
DR   OMA; TIKHYSN; -.
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: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   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.
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          343..491
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   498 AA;  56524 MW;  F43E702F497DBC0A CRC64;
     MTKIKFNSGL LKQIWNYSEL PQTGISLRQM CQFGANPNPA TLFKASCFVL RELPIRLAHR
     IKELESLPNG LNKMNDVIQV RDWYTQSFKE LYEFAHDRST SNGKLYQMLY GGLEPDTPME
     SEVLRNIIQL CYRDEELDSK HGRSNTSVPH RNTFVDDGLV VTKRKWSVSN QSLSSSRGQV
     LTPKKYYSSP LVTSLEVWPK EILKFNAALF KVLHNIKVRH NATVVTLAKG VLKWKKTCQQ
     NMFDDSVQSF LDRFYMSRIG IRMLIAQHLD LLEPSLHCQN GKSDSYVGSI CTKTNITQIA
     EDAIDNAKLI CSEHYGLFEA PEVELLCFPK NATGLNNEIE FMYVPGHLIH MLVETLKNAL
     RATVEKTVES NPGMDVYDLK FPHVKVIICE GLEDITVKIS DEGGGIARSN LPLIWTYLYS
     TMPDDCQLEL MKDECDENPR VSSFVNNVPL AGYGYGLALS RLYARYFGGD LKLISMEGFG
     TDVYLHLNRL STSSEPLQ
//
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