ID A3GI33_PICST Unreviewed; 517 AA.
AC A3GI33;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=BCK4 {ECO:0000313|EMBL:EAZ63163.2};
GN ORFNames=PICST_29203 {ECO:0000313|EMBL:EAZ63163.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ63163.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ63163.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAZ63163.2}.
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DR EMBL; AAVQ01000002; EAZ63163.2; -; Genomic_DNA.
DR RefSeq; XP_001387186.2; XM_001387149.1.
DR AlphaFoldDB; A3GI33; -.
DR STRING; 322104.A3GI33; -.
DR GeneID; 4851932; -.
DR KEGG; pic:PICST_29203; -.
DR eggNOG; KOG0787; Eukaryota.
DR HOGENOM; CLU_023861_0_1_1; -.
DR InParanoid; A3GI33; -.
DR OMA; ICEAQEH; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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 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; 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}; Pyruvate {ECO:0000313|EMBL:EAZ63163.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 116..278
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT DOMAIN 328..503
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF02518"
SQ SEQUENCE 517 AA; 58739 MW; BD4C2A60E670789A CRC64;
MTHLTPFSIH KTAAYENSFI CTMQAPAMLQ TARIQKHCSR SCGSISVLVR GYSSEHSPIT
AHSYINDDFL STISKQEIAK HLKNLGPFPT YSNILNQQHF YQNEVLMEYS KRDPHPVSLR
QLAGYGNKLT KQKILNSANF VRIELPIRLA IRIRDLQTLP FGVVNNFHLA QIYESYYHSF
NAFRKIPQIN TLDQNDKFCE TLSSLLDDHV FNLSHLMMGA LEVSILNNLG REELDNFMSS
MLRSRISRRV IVEEHLSLSE NYRSNPYAVK PPHYLGEIFH DCKAIDHFKI VADMIKKSMV
SIFPNIDNMP DLEIEGDLST SFPFMVPHLH YLLSEILRNS YEATIKTHAK MTSKKLPSIR
ITIINLKKEV IFRISDQGGG ISHDQLKSVW SFCKAPDLAR NSLANFHRIP GLQLYSNLKV
TPAGSSIVSN ANSQKLLSST SLDDVDASTK KKKSTLDRLI DRPYENKLGL GLPMCKVYAD
YWNGELTMNS LEGYGSDTSL TLKKLGYHSN VMQLDRA
//
