ID A0A1W5CR28_9LECA Unreviewed; 807 AA.
AC A0A1W5CR28;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM33296.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003747}.
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 -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}.
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DR EMBL; FWEW01000007; SLM33296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5CR28; -.
DR OrthoDB; 1789758at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR38248:SF2; FUNK1 11; 1.
DR PANTHER; PTHR38248; FUNK1 6; 1.
DR Pfam; PF17667; Pkinase_fungal; 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 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:SLM33296.1};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000313|EMBL:SLM33296.1}.
FT DOMAIN 424..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 90967 MW; B236003A32C52A25 CRC64;
MAHLNREERD AINEYPLGDS LSGVREALRE AERNTHYEAS QSDDSADAPE RPRLFVAAIE
KLLFSILSPS KVSVALASRT GRETLGVDLM VLRLRVEKGD FEYKHFRPLS QLVIKQAPDV
DIWAAVVALV RLVSYSSPPP SLPPSFDTPI THTSASQQGS EQTRREIEHR VFEEIRHCTH
RAVEGFHEKY FEGQKWNRRA KRIWQSAKSR YSDSDKRWTQ LPAAATQDEV WAWLLNLQQE
LLATERAGYF TSDLSNKVGA EASRQLDLLV KMRSNEAAGE KHDWRDVLVI GELKKSDQKD
KRLWLQVGSA VRNVFASQPT RLFVHAFTLT GTEMETWIFD RSGPYSGATF DVHEEPEKFI
QVMCAYLMMS DEELGLDTFI KAKDNRLFVS MPVEVRGKMR NRQLELDPNP IAHQRAIVCR
GTSCFLAKAA GAAEFDRVVK YSWTSSMRPP EADLLNKANE RGVKGLAKVV GYHEEVTSIS
RLREGLVFST PHKFRGVPRS ANTSFSQSQP PLNHPFSQFY GLSIASKGHS KGKSTDCSSH
PSKRSQSNSQ LAKTEQAENG VSYPVQKPQG TSLVQQDLAP YDNRILRILA ISPAGRSISQ
FKSVVELLEG LRDALKVHRS LYMDGKILHR DISENNIIIT DPGMADGFKG MLIDLDLAKE
EGKGPSGARH RTGTMEFMAI EVLQGTSHTY RHDIEAFFYV LIWLCARRGW ALAGTSKKPP
TETILSHWYT GTYKDIARNK RGDMDKDGLE VILEECSQVF DCVKPLCRII RDVLFSYNRL
FTGTPQDPNI LYDPIIEAFD DTISGLG
//
