BUD32_CRYNJ
ID BUD32_CRYNJ Reviewed; 289 AA.
AC P0CP72; Q55K29; Q5K9H0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=EKC/KEOPS complex subunit BUD32;
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q9UYB9};
DE AltName: Full=Atypical serine/threonine protein kinase BUD32;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53323};
GN Name=BUD32; OrderedLocusNames=CNK01970;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase
CC activity in the context of the EKC/KEOPS complex and likely plays a
CC supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex
CC also promotes both telomere uncapping and telomere elongation. The
CC complex is required for efficient recruitment of transcriptional
CC coactivators. {ECO:0000250|UniProtKB:P53323}.
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:0000250|UniProtKB:P53323};
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:0000250|UniProtKB:P53323};
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:0000250|UniProtKB:P53323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53323}. Nucleus
CC {ECO:0000250|UniProtKB:P53323}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:P53323}.
CC -!- DOMAIN: This protein is considered an atypical serine/threonine kinase,
CC because it lacks the conventional structural elements necessary for the
CC substrate recognition as well as a lysine residue that in all other
CC serine/threonine kinases participates in the catalytic event (By
CC similarity). BUD32 has protein kinase activity in vitro, but in the
CC context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches
CC the activity of BUD32 from kinase into ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW46242.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE017351; AAW46242.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_567759.1; XM_567759.1.
DR AlphaFoldDB; P0CP72; -.
DR SMR; P0CP72; -.
DR STRING; 214684.P0CP72; -.
DR InParanoid; P0CP72; -.
DR OrthoDB; 1425238at2759; -.
DR Proteomes; UP000002149; Chromosome 11.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IBA:GO_Central.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR12209; PTHR12209; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Chromosome; Cytoplasm; Hydrolase; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transcription;
KW Transcription regulation; Transferase; tRNA processing.
FT CHAIN 1..289
FT /note="EKC/KEOPS complex subunit BUD32"
FT /id="PRO_0000278912"
FT DOMAIN 8..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 134..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 289 AA; 31670 MW; 5163B24144B287DF CRC64;
MAASTPLLSR GTLIKQGAEA KVYALPSLFP EPTTYHPGSS SSFSAASPTP VILKHRFTKT
YRHPTLDASL TSQRLTFEAR ALARAAKAGV TVPKVVWVDE KAGVIGMERI EGWSVREILG
GGAEGEVEVI EEQEIEEDVE NKAEDSAVRE EPEGPESEGL KALKNLGVTQ EHLMRSIGAA
LARLHKTMII HGDLTTSNMM VRLTPGGSGP YEIVLIDFGL SSQAQFPENY AVDLYVLERA
FASTHPRSEK LYAGVLETYA EGLGEKKWKP IQIKLKDVRR RGRKRDMTG
