ID C5DD76_LACTC Unreviewed; 265 AA.
AC C5DD76;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=EKC/KEOPS complex subunit BUD32 {ECO:0000256|ARBA:ARBA00019973};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Atypical Serine/threonine protein kinase BUD32 {ECO:0000256|ARBA:ARBA00030980, ECO:0000256|ARBA:ARBA00033194};
DE AltName: Full=EKC/KEOPS complex subunit bud32 {ECO:0000256|ARBA:ARBA00013948};
GN OrderedLocusNames=KLTH0B08954g {ECO:0000313|EMBL:CAR21737.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21737.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR21737.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC {ECO:0000256|ARBA:ARBA00011534}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000256|ARBA:ARBA00010630}.
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DR EMBL; CU928166; CAR21737.1; -; Genomic_DNA.
DR RefSeq; XP_002552175.1; XM_002552129.1.
DR AlphaFoldDB; C5DD76; -.
DR STRING; 559295.C5DD76; -.
DR GeneID; 8291018; -.
DR KEGG; lth:KLTH0B08954g; -.
DR eggNOG; KOG3087; Eukaryota.
DR HOGENOM; CLU_063953_1_1_1; -.
DR InParanoid; C5DD76; -.
DR OMA; HKLYMEY; -.
DR OrthoDB; 121617at2759; -.
DR Proteomes; UP000002036; Chromosome B.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR NCBIfam; TIGR03724; arch_bud32; 1.
DR PANTHER; PTHR12209:SF0; EKC_KEOPS COMPLEX SUBUNIT TP53RK; 1.
DR PANTHER; PTHR12209; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF06293; Kdo; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 16..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 265 AA; 30236 MW; 4EF25B9CCCD88B02 CRC64;
MSKEVIEQVV TYLTPNVPIV PISQGAEAFV FTTNVHPYNA SACKTAGDIP VKYIIKYRPP
KKYRHPSIDK TLTKHRTLSE SRILAKLSQV PGLHVPKLIA CDVYNGCIWI EFIGEDLPES
HGFSNLKNFL WMYKTDPYNI AVEKVLFKVG EQIGLLHWND YCHGDLTTSN LVLHQENGDW
SPYLIDFGLG SASTLVEDKG VDLYVLERAI ISTHSKFADK YNEWILMGFK SVYENEGKKG
QQKLKDVIKR FEEVRLRGRK RSMLG
//
